32nd Annual Symposium BOSTON July 9 - 12, 2018 Program

www.proteinsociety.org Table of Contents #PS32

2 Welcome Mission 3 Program Planning Committee 4 Committees

The Protein Society is a not-for-profi t scholarly society 7 Corporate Support with a mission to advance state-of-the-art science through international forums that promote commu- 8 Registration nication, cooperation, and collaboration among scientists involved in the study of proteins. 9 Hotel Floor Plan

For 32 years, The Protein Society has served as the in- 11 General Information tellectual home of investigators across all disciplines - and from around the world - involved in the study 16 2018 Protein Society Award Winners of protein structure, function, and design. The Soci- ety provides forums for scientifi c collaboration and 22 Travel Awards communication and supports professional growth of young investigators through workshops, networking 24 At-A-Glance opportunities, and by encouraging junior research- ers to participate fully in the Annual Symposium. In 26 Program addition to our Symposium, the Society’s prestigious journal, Protein Science, serves as an ideal platform 40 Exhibitor Director to further the science of proteins in the broadest sense possible. 50 Poster Presentation Schedule

64 Abstracts: TPS Award Winners & Invited Speakers

86 Posters #PS32 1986 - 2018 1 Welcome Program Planning Committee #PS32 Welcome to Boston and to the 2018 32nd Boston | July 9 - 12, 2018 Annual Symposium of the Protein Society! We are excited to bring you this year’s Annual Symposium comprising twelve exceptional scien- tifi c sessions that cover a wide range of scientifi c achievement in the fi eld of protein science. Our program committee, chaired by Susan Marqusee, MD, Ph.D., and James Fraser, Ph.D., has convened a host of stimulating speakers and topical areas of current research. This year’s Symposium continues our commitment to open participation with nearly 30% of Symposium talks coming from contributed sessions and speakers across a broad range of topics, an amazing line-up of poster presentations during our poster sessions, and continued recognition of outstanding young scientists through specially-designated sessions and awards. Susan Marqusee, M.D. Ph.D. James Fraser, Ph.D. Award winners will also present their work throughout the Symposium, which Co-Chair Co-Chair is not to be missed! However, if you cannot make it to all talks, you can read UC San Francisco about their work in a future special issue of Protein Science, the Society journal. UC Berkeley Finally, I personally encourage you to participate in the numerous activities we’ve planned for Boston – from mixers and social events, including a Red Sox game, to mentoring and education panels, and our Members' Reception (which is open to all).

While we celebrate more than 3 decades of impact in the fi eld of protein science, future challenges drive us to advocate for the importance of scientifi c research in the United States and throughout the world. I urge you to engage in important dialogues within our community and, of growing importance, with the public, on the critical need for scientifi c research.

Thank you for joining us in our 32nd Annual Symposium in Boston. We hope you will take advantage of everything our event has to offer. Finally, we would Allan Drummond, Ph.D. Deborah Fass, Ph.D. appreciate it greatly if you will take a few moments to give us your feedback U Chicago Weizmann Institute of Science and suggestions for improvement in the survey you’ll receive at the end of the conference. We are committed to strengthening our events to meet the needs of members and constituents, and your honest feedback will directly shape future events.

Wishing you all a fruitful and engaging Symposium. Please take a moment to introduce yourselves to me during the meeting; I would love to meet you.

Kind Regards,

Charles L. Brooks III, Ph.D. Jeanne Hardy, Ph.D. Kresten Lindorff-Larsen, Ph.D. President U Mass Amherst U Copehhagen 2 3 Nominating Committee Education Committee #PS32 Committees Heather Pinkett, Ph.D. (Chair) Matthew Gage, Ph.D. (Chair) Northwestern University University of Massachusetts Lowell Executive Council Bil Clemons, Ph.D. Shanadeen Begay, Ph.D. California Institute of Technology President Councilor Mary Munson, Ph.D. Northeastern University Charles L. Brooks III, Ph.D. University of Massachusetts Tijana Grove, Ph.D. University of Michigan Medical School Virginia Tech AJitha Cristie-David University of Michigan President-Past Councilor Satoshi Takahashi, Ph.D. Jeanne Hardy, Ph.D. Carol Post, Ph.D. Tohuku University University of Massachusetts Rochelin Dalangin Purdue University University of Alberta Councilor Gunnar von Heijne, Ph.D. Elizabeth Rhoades, Ph.D. University of Pennsylvania Secretary/Treasurer Stockholm University Elizabeth Komives, Ph.D. University of California, San Diego Jean Baum, Ph.D. Tobin Sosnick, Ph.D. Councilor Grant Walkup, Ph.D. Rutgers University University of Chicago Agios Pharmaceuticals Daniel Kraut, Ph.D. Villanova University Councilor Doug Barrick, Ph.D. Corey Wilson, Ph.D. Johns Hopkins University Yale University Ex-Officio Members James Lipchock, Ph.D. Councilor Patricia Clark, Ph.D. Mentoring Committee Washington College University of Notre Dame Editor-in-Chief Brian Matthews, Ph.D. Protein Science Stephen Fuchs, Ph.D. (Chair) Robert McFeeters, Ph.D. Councilor Erin Dueber, Ph.D. University of Oregon Tufts University University of Alabama, Huntsville Genentech Executive Director Raluca Cadar Matthew Cordes, Ph.D. Kathryn McMenimen, Ph.D. University of Arizona Councilor Donald Hilvert, Ph.D. The Protein Society Mount Holyoke College ETH AJitha Cristie-David Denise Okafor, Ph.D. University of Michigan Councilor Elizabeth Komives, Ph.D. Emory University University of California - Giovanna Ghirlanda, Ph.D. San Diego Arizona State University

Councilor Brian Kuhlman, Ph.D. Jeffrey Haas, Ph.D. University of North Carolina - Monsanto Chapel Hill Manasi Pethe, Ph.D. Scripps Research Institute Councilor Elizabeth Meiering, Ph.D. University of Waterloo Taylor Stewart Tufts University

Eric Sundberg, Ph.D. University of Maryland Medical School

Andrew Vendel, Ph.D. 4 Eli Lilly 5 Committees Corporate Support #PS32 The Protein Society is extremely grateful to the following sponsors Abstract Review Committee for their generosity and continued support:

John Osterhout, Ph.D. (Chair) Cesar Ramirez-Sarmiento, Ph.D. Angelo State University Pontifi cal Catholic University of Chile GOLD Jeanine Amacher, Ph.D. Philipp Schmidpeter, Ph.D. Western Washington University Weill Cornell Medical College SPONSORS Rodney Austin, Ph.D. Karl Schmitz, Ph.D. Geneva College, PA University of Delaware

Matthew Gage, Ph.D. Brian Shilton, Ph.D. University of Massachusetts Lowell University of Western Ontario

Sajith Jayasinghe, Ph.D. Christopher Snow, Ph.D. California State University San Marcos Colorado State University

Constance Jeffery, Ph.D. Jeffrey L Urbauer, Ph.D. University of Illinois, Chicago University of Georgia

Peter Kahn, Ph.D. Jill Zeilstra-Ryalls, Ph.D. Rutgers University Bowling Green State University

Prem Kumarathasan, Ph.D. Health Canada

Jinsong Liu, Ph.D. MD Anderson SILVER Sanela Martic, Ph.D. Oakland University SPONSORS

Carrie Partch, Ph.D. University of California Santa Cruz

Sebastian Pechmann, Ph.D. University of Montreal

Kay Perry, Ph.D. Thank you for helping us celebrate 32 years of impact. Argonne National Laboratory 6 7 #PS32

9

Posters Exhibits & & Exhibits Hotel Floor Plan Lower 8:30 a.m. - 12:00 p.m. 5:00 p.m. - 8:00 7:30 a.m. - 6:30 p.m. 7:30 a.m. - 6:30 p.m. 8:30 a.m. - 7:00 p.m. fi cation, the name badge is required

Hours Sunday, July 8: Monday, July 9: Tuesday, July 10: Wednesday, July 11: Thursday, July 12: Badge/Delegate Pickup Badge/Delegate All registrants must go to the Symposium Registration Desk on Level . All attendees are required to wear their badge at all times. In ad- dition to being a means of identi for admission to all Symposium-related events. Registration The Registration Area will open at 5:00 p.m. on July 8 (refer to hours below). Registration includes admission to all scienti fi c and poster sessions, exhib- its, and one t-shirt. Registration does not include any meals. 8 #PS32 11 cate of attendance via email in PDF fi internet access for the Symposium in fi cials of The Protein Society, or their representatives, fi format after the Symposium. for editorial and promotional purposes, on the Society website, social media outlets, and publications. Recordings of any kind (audio taping, videotaping, camera, tablets, or cell phones) in the session rooms, Exhibit Hall, and poster areas are strictly prohibited, unless accompanied by a member of the Society staff. Any individual seen taking photographs any session or presentation will be escorted out by security. meeting space. Please use the following information to gain access: Network Name: PS32 Password: PS322018 Live Mobile App The PS32 Mobile App provides on-the-go Symposium information including a program planner, poster presentations info, exhibitor list, social media updates, #PS32 alerts, and maps. The Protein Society’s “PS 32” mobile application is available for download in the Apple App Store and Google Play. You can view/create schedules; view abstracts, and interact virtually with speakers using the app. Cameras/Video Recording The unauthorized use of cameras/video recording inside session rooms or among the posters is prohibited. Mobile Devices As a courtesy to your fellow attendees, please silence all cell phones prior to entering a session room. Certificates of Attendance All attendees will receive a certi Internet Access There is complimentary wi- Photography Registration for the meeting implies consent to having photographs taken and to their use by of General Info 10 Hotel Floor Plan General Info General Info #PS32 Poster Set Up & Removal Social Media The poster set-up is taking place on the day of your presentation. The Society staff will be updating its Facebook page, Instagram, and Posters are displayed on a stan-dard poster board with the dimensions Twitter feed with Annual Meeting information throughout the meeting. of 90 inches (2.3 meters) wide by 42 inches (1.1 meters) high of usable Follow us on: Facebook: www.facebook. com/ProteinSociety; www.insta- space. Each poster presenter is responsible for removing his own poster gram/proteinsociety; Twitter: @ProteinSociety, use hashtag #PS32. at the end of the Session. We will dispose of any posters that are left behind.

Public Transportation Poster Viewing Times Rail Posters are on display from Monday morning until Wednesday evening Amtrak services Boston, New York, Washington, DC, Philadelphia, Balti- in the Exhibit and Poster Hall (Gloucester Room). During the following more & nationwide from Boston's South Station or Back Bay Station. shifts, exhibitors will be on hand, and a Mix & Mingle networking recep- tion will take place: Take the T Monday, July 9: 11:30 a.m. - 1:30 p.m. Boston's public transportation system is operated by the Massachusetts 4:30 - 6:30 p.m. - Presentations Bay Transportation Authority, but locals know it simply as the "T".It offers subway, bus, trolley car and boat service to just about everywhere in the Tuesday, July 10: 11:30 a.m. - 1:30 p.m. Greater Boston area and beyond. To ride the T, you need to purchase a 4:30 - 6:30 p.m. - Presentations CharlieCard or CharlieTicket. These can be purchased at every subway station at vending machines and at select convenience stores. The basic Wednesday, July 11: 11:30 a.m. - 1:30 p.m. fare is $2.75 with a CharlieTicket or $2.25 if you have a Charlie Card. 5:30 - 7:30 p.m. - Presentations

Taxi Taxi service is available throughout the city. From Logan International Airport to the Boston Marriott Copley Place taxi fares are approximately $40, one way.

12 13 TPS Membership Benefits Include: #PS32 Annual Symposium and Awards • Members save as much as 50% for the Annual Symposium • Get funding for your local protein-centered mini-symposium, workshop, or other event with a Member Mini-Grant • Connect with TPS leaders and have a say in the direction of your Society • Only members can submit or sponsor an abstract for the Best Poster Com- petition • Nominate your colleagues for one of seven prestigious TPS awards • Eligibility to submit a contributed talk or be considered for a Young Inves- tigator Talk • Design your own session at an upcoming Symposium

Protein Science Benefits • Complimentary online access to the premier Journal focused on all aspects of protein science • $250 discount on publication fees • Pain-Free Publishing: Fast turnaround under the guidance of Edi- tor-in-Chief Brian Matthews • Reduced open-access fees from publisher Wiley Blackwell

Networking and Leadership • Connect and collaborate privately with other members through the Individual Memberships Member Directory or the members-only LinkedIn group TPS members represent an international community of all those who share an inter- • Be eligible to vote – or stand yourself – for TPS Executive Council, est in the structure, function, design, synthesis, and utilization of proteins. In fact, it is Nominating Committee, and other leadership roles this diversity of disciplines and perspectives represented by TPS members that is the • Stay informed with the monthly member e-news group’s defi ning characteristic.

Members include chemists, biologists, physicists, and mathematicians - Legislative Action researchers of all stripes, whose collaboration and communication comprise • Public affairs representation through FASEB the Society’s core mission. They represent academia, industry, government, non-profi ts, and leading institutions in more than 50 nations.

14 15 Susan Marqusee, MD, Ph.D., University of California - Berkeley #PS32 2018 Protein Society 2018 Dorothy Crowfoot Hodgkin Award Winner - Sponsored by Genentech

The 2018 recipient is Professor Susan Marqusee. Dr. Award Winners Marqusee, a biophysical chemist whose work focuses Raymond Stevens, Ph.D., University of Southern California on protein folding and dynamics, is one of the 2018 Stein & Moore Award Winner world’s top experimental scientists in the fi eld of pro- tein folding. Her work has led to the most complete The 2018 recipient is Professor Raymond Stevens (Univer- characterization of a protein energy landscape and sity of Southern California). Dr. Stevens has pioneered provided a rigorous and unprecedented detailed the development of membrane protein structural analysis of the diffusion of a folding protein on this biology technologies including nanoliter crystallization energy surface, validating in this manner the hier- robotics, nanoliter imaging, micro-expression and archical model of protein folding. She is known for screening of constructs, thermal stability analysis, and many contributions, including the fi rst de novo design the fusion partner tool chest that led to the ground of a short peptide that folded into a specifi c structure breaking seminal work on the structures and mecha- (alpha helix), the application of novel hydrogen nistic understanding of the G protein-coupled receptor exchange methods to measure rare partially-struc- superfamily. His latest and quite possibly most impactful tured conformers, and the mechanical manipulation endeavor is to create the fi rst atomic model of the of single-protein molecules. Her work has produced human body that can be used for testing drugs without the most detailed view of the energy landscape of any risk to patients’ health. He founded six biotech- a protein. Her work impacts areas of biology ranging nology companies focused on structure-based drug from deciphering the effects of genome variation to design and was involved in the development of several the mechanism of protein misfolding pathologies. marketed drugs to treat a number of different human diseases. Dr. Stevens also founded two research insti- Jane and Dave Richardson, Duke University tutes - iHuman Institute in Shanghai, China and Bridge 2018 Carl Brändén Award Winner - Sponsored by Rigaku Corp. Institute in Los Angeles, CA. The 2018 recipients of this award, Jane & Dave Rich- ardson have been involved in many groundbreaking Yifan Cheng, Ph.D., University of California, San Francisco developments through the years, including solving two 2018 Christian B. Anfinsen Award Winner of the fi rst 20 protein crystal structures (Staph nuclease & Cu,Zn superoxide dismutase); early work in what is The recipient of this award in 2018 is Professor Yifan now called structural bioinformatics: (beta bulges, Cheng. Dr. Cheng is considered one of the world’s Greek key folds, helix caps, etc.); developing the top few experts in high-resolution cryo-EM. He has ribbon drawing, still widely used to represent 3D pro- been involved in various groundbreaking techno- tein folds both on the page and in 3D graphics -- the logical developments that greatly advanced single hand-drawn TIM barrel ribbon schematic was Picture particle cryo-EM and its application in studying inte- of the Day on Wikipedia Nov 19, 2009; pioneering ear- gral membrane proteins. He has also been involved ly protein de novo design in the 1980s with Betabellin in the structural studies of TRP channels. In particular, and Felix; pioneering interactive 3D macromolecular Dr. Cheng has been involved in the determinations graphics for small personal computers with the Mage/ of TRPV1 ion channel, the fi rst atomic structure of kinemage system, fi rst used as digital supplements at an integral membrane protein determined by single the launch of Protein Science, then for the Branden & particle cryo-EM, and the determination of the Tooze textbook, and later online with KiNG; develop- atomic structure of TRPV1 in lipid nanodisc, the fi rst ing the method of all-atom contact analysis, which adds explicit hydrogen positions membrane protein atomic structure in a lipid bilayer to analyze packing inside and between macromolecules. It diagnoses and helps by single particle cryo-EM. These studies had major correct local modeling problems in protein and RNA structures. They were also impact on structural biology of membrane proteins, involved in developing and updating the MolProbity validation web service, now and methods developed in these studies are now used by most crystallography labs, within the Phenix software system, at deposition to widely used in structural studies of a broad range of the worldwide Protein Data Bank, and in crystallography courses; and are currently integral membrane proteins. developing new validation methods suitable in the 2.5-4Å resolution range, for crys- tallography and especially for modern cryoEM. 16 17 #PS32 David Baker, Ph.D., University of Washington 2018 Protein Society 2018 Hans Neurath Award Winner

In 2018, the Hans Neurath Awardee is Professor David Award Winners Baker. Dr. Baker’s scientifi c achievements have put him at the forefront of many disciplines in computa- Michael Rosen, Ph.D., University of Texas SW Medical School tional protein science over the past decade. Some 2018 Emil Thomas Kaiser Award Winner of these achievements have included: Advances in The 2018 recipient is Professor Michael Rosen. Dr. de novo protein design and protein structure predic- Rosen has been a leader in deciphering how mac- tion of thousands of proteins of unknown structure romolecular phase separation organizes eukaryotic using Rosetta atomistic modeling and evolutionary cells through formation of biomolecular condensates, couplings; atomistic refi nement of x-ray crystallo- compartments that concentrate proteins and RNA graphic structures, which has been packaged in the without a surrounding membrane. Of greatest current most popular software suite for x-ray crystallography, impact is his seminal work on liquid-liquid phase sep- PHENIX; and reproducible design of stable, atomi- aration in cells and how the resulting membrane-less cally accurate, small proteins, which may be used as organelles participate in fundamental cellular binders and inhibitors. These breakthroughs required physiology. His group showed that diverse multiva- many additional technical advances in modeling lent molecules, including natural and engineered and experimental characterization, and they reduce multidomain proteins, intrinsically disordered proteins to practice what was for many decades the holy and nucleic acids, undergo phase separation in vitro grail of protein science: fundamental understanding and in cells, forming distinct structures with unique of the determinants of protein structure and stability functions. Further, they demonstrated how covalent that leads to consistent predictive capabilities, modifi cations can control the formation and disso- including the ability to design protein shapes and lution of condensates and provided initial models to functions as desired. explain condensate composition. Dr. Rosen’s work has important implications for protein chemistry, Dr. Baker will speak at the 2019 Annual Symposium in biophysics and cell biology, and for human diseases Seattle, WA. such as neurodegenertion and cancer.

Brandon Ruotolo, Ph.D., University of Michigan 2018 Protein Science Young Investigator Award Winner - Sponsored by Wiley The 2018 recipient is Professor Brandon Ruotolo (Uni- versity of Michigan). Dr. Ruotolo, Associate Professor of Chemistry, has made continual and substantive contributions to our understanding of protein structure in the absence of bulk solvent, performing pioneering ion mobility-mass spectrometry measurements on model peptide, protein and multi-protein complex systems that have illustrated the level of conformational memory retained by biopolymers in the gas phase. Ruotolo is also responsible for the creation of new measurement technologies that have furthered our understanding of protein biophysics and structure. Most recently, Ruotolo has spearheaded the development of collision induced unfolding for the rapid analysis of protein complex struc- ture and stability and demonstrated the utility of such experiments for applications ranging from conforma- tionally-selective inhibitor screening to the characteriza- tion of biotherapeutics. 18 19 #PS32 Protein Science Best Paper Award Winners Minfei Su, North Dakota State University Chang-TingC Lin, Johns Hopkins University 2018 Best Paper Award Winner 2018 Best Paper Award Winner Chang-Ting Lin, worked with Taekjip Ha, who Minfei Su grew up in Jiangsu Province, China. describes him as follows: “Chang-Ting came from She obtained a MS in Botany from Nanjing Uni- Taiwan where he had signifi cant research experi- versity a nd a BS in Biotechnology from the Nan- ences on G-quadruplex forming DNA using more jing Agricultural University where she received traditional biophysical techniques. During his PhD, multiple accolades including “Best-all-round Stu- he had to move with me to Baltimore. Because dent Scholarship” and “Outstanding Graduate." his instrument combining total internal refl ection In 2010, she was admitted to the Ph.D. program fl uorescence microscopy with optical tweezers for in the Biochemistry Department at North Dakota examining protein movements on long stretched State University, where she started her graduate nucleic acids had been built by a previous phys- studies. As she recalls “during my rotation in ics student, he had no prior knowledge on how Dr. Sangita Sinha’s lab, I was fascinated by the to rebuild the instrument upon lab relocation. He beautiful atomic structures of proteins solved worked very hard with a senior postdoc to teach by X-ray crystallography and how the structural himself and took the instrument apart and rebuilt details of proteins correlate to their functions. I it a couple of times in Illinois before he packed joined Dr. Sinha’s lab and started to work on everything up. He was successful in rebuilding the structures of proteins involved in autophagy, instrument. a catabolic pathway essential for organismal homeostasis in all eukaryotes. I am very appre- Chang-Ting is an excellent speaker and always ciative of the guidance and support from Dr. gives engaging talks. As part of the PhD require- Sinha over the years which helped me develop ment, he gave a talk to the department on opto- commitment towards pursuing a career in aca- genetics using the light-oxygen-voltage-sensing demia. I graduated from Dr. Sinha’s lab in 2016 (LOV2) domain. He was then inspired to engineer and am now a postdoc at Weill Cornell Medical a helicase with LOV2 so he could control the College.” enzyme activity by light. It is still in an early stage but the project has a high risk and high reward fl avor and because he was able to publish his fi rst author paper in Protein Science last year, he was able to start this ambitious project.”

20 21 #PS32

23 Max Planck Institute of Colloids and Interfaces University of Michigan Indian Institute of Technology Madras University of Michigan University of California, San Francisco , Carleton University Agriculture and Agri-Food Canada ETH Zurich Bethune Cookman University Emory University Emory University University College London Harvard University , The Pennsylvania State University Weizmann Institute of Science Brown University CUNY Advanced Science Research Center , Brown University University of Illinois, Chicago Peking University Lawrence Livermore National Laboratory Oakland University 8 Protein Science Tr a vel Award Recipients 2 0 1 8 Protein Aaron Bozzi, Igor Dikiy, Wei He, Fuguo Jiang, University of California, Berkeley Tilmann Kuenzl, Denise Okafor, Bikash Sahoo, University of Michigan Francesca Anson, University of Massachusetts, Amherst Henriette Autzen, Ana Barran , University of Florida Christine Childers Adam Chin-Fatt, Nuria Codina, Ajitha Cristie-David, Denise Okafor, Cynthia Okoye , Williams College Arumay Pal, Stanislav Pekov, Moscow Institute of Physics and Technology Theerawat Prasertanan, University of Saskatchewan Jörn Schmiedel, Centre for Genomic Regulation (CRG) Roman Sloutsky, University of Massachusetts, Amherst John Strahan , Amherst College Miranda Villanueva , Williams College Nina Wolf, Ailin Wang Yansheng Ye Iva Ziu, Outstanding Promise Tr a vel Awards 2 0 1 8 Hans Neurath Aakriti Gautam, Matthew Henley, Nancy Hernandez, Rutgers University Sherlyn Jemimah, Maryam Kashefi, University of Massachusetts Amherst Hengyi Li, Mark Liang, Patricia Lopez-Garcia,

fi t from our Annual Meeting by A w ard s . The leadership and Executive Council Aston University vel Award Recipients a vel Award University of Arizona UConn Health Chapman University School of Pharmacy University of Ottawa University of Copenhagen Rensselaer Polytechnic Institute Monash University Oakland University University of Massachusetts Amherst Ferreira-Amaral, r a vel of The Protein Society also THANKS the recent donors to Finn Wold Travel Awards Fund. The Protein Society would also like to recognize the Hans Neurath Foundation for supporting the generous Hans Neurath Outstanding Promise Travel awards and Wiley , for supporting the Protein Science travel awards. Matthew Bienick, Noreen Ahmed, Taibah Aldakhil, Saba Anwar, Benjamin Brandsen, University of Washington Sean Crowe, Eva Gerber , Yale University Raghupathi Kummari, ACTREC, TATA Hospital, HBNI, Kharghar Mukesh Mahajan , University of Michigan Zeinab Moussa, University of Houston Dennis Özcelik, Gerardo Perez-Goncalves , University North Carolina at Chapel Hill Ngoc Thu Hang Pham, INRS - Institut Armand-Frappier, Universite Du Quebec Fabian Sesterhenn, Institute of Bioengineering, École Polytechnique Fédérale de Lausanne Jane Thibeault, Gabrielle Valles, Saboora Waris, Tingting Xu , Guangzhou Institutes of Biomedicine and Health,Chinese Academy of Sciences 22 Finn Wold Tr Wold 2 0 1 8 Finn Marta M. T Congratulations to the following outstanding students and early-career investigators for receiving travel assistance to attend The 32nd Annual Symposium of The Protein Society. Under the strong belief that our Symposia presents an invaluable opportunity for future protein scientists, The Protein Society is committed to making it possible for young scientists to participate and bene awarding the Finn Wold Travel Awards At A Glance

24 25 #PS32 CONCURRENT MORNING SESSION 2 Proteins See the Light! Triggered Conformational and Functional Changes Program 9:40 - 11:30 a.m. |Salon F Day 1 - Monday, July 9, 2018 9:40 - 9:45 a.m. Introduction From Chair Michael Thompson, University of California; Opening Plenary Session San Francisco, United States 8:30 - 9:10 a.m. | Salons E and F 9:45 - 10:15 a.m. A Shape-Shifting Protein Coordinates Timekeeping by 8:30 - 8:35 a.m. Intro & Welcome from The Protein Society President the Cyanobacterial Circadian Clock Charles L. Brooks III, University of Michigan Carrie Partch, University of California, Santa Cruz; California, United States 8:35 - 8:40 a.m. Presentation of the 2017 Christian B. Anfi nsen Award to Lewis Kay 10:15 - 10:45 a.m. Circadian Rhythms from Coupled ATPase Domains Mike Rust, The University of Chicago 8:40 - 9:10 a.m. Solution NMR: Why Bother? Illinois; United States Lewis Kay, University of Toronto, Canada 10:45 - 11 a.m. Interplay Between Active and Inactive States in Coffee Break | 9:10 - 9:40 a.m. |Gloucester Light-sensing Histidine Kinase EL346 Igor Dikiy, The City University of New York Advanced CONCURRENT MORNING SESSION 1 Science Research Center; New York, United States Propagating Aggregated Conformational States 9:40 - 11:30 a.m. |Salon E 11 - 11:30 a.m. A Molecular Movie of Structural Changes in the Light-Driven Proton Pump Bacteriorhodopsin 9:40 - 9:45 a.m. Introduction from Chair Eriko Nango, Spring-8/SACLA; Kyoto, Japan Dennis Özcelik, University of Copenhagen, Denmark LUNCH 9:45 - 10:15 a.m. Remembering the Past: A New Form of Protein- 11:30 a.m. - 1:30 p.m. Based Inheritance Networking Lunch (RSVP-ONLY EVENT) | Third Floor Atrium Dan Jarosz, Stanford University; California, United States Boxed Lunch Pick Up Station |Gloucester

10:15 - 10:45 a.m. Amyloids: From the Origin to the End of Life Poster Displays & Exhibits Open |Gloucester Roland Riek, ETH; Zurich, Switzerland

10:45 - 11 a.m. Quantifying Nucleation In Vivo Reveals the Physical Basis of Prion-Like Phase Behavior Randal Halfmann, Stowers Institute for Medical Research; Missouri, United States

11 - 11:30 a.m. The Formation of Functional Amyloid Fibrils by Viral Proteins that Modulate Host Cell Death Pathways; Margaret Sunde, University of Sydney; Australia

26 27 CONCURRENT AFTERNOON SESSION 4 #PS32 Proteins in Control of Membranes Program 1:30 - 4:30 p.m. |Salon F 1:30 - 1:35 p.m. Introduction from Chair Day 1 - Monday, July 9, 2018 Elizabeth Draganova, Tufts University; Massachusetts; United States CONCURRENT AFTERNOON SESSION 3 Creativity in Drug Discovery 1:35 - 2:05 p.m. Structural and Mechanistic Studies on the Dynamin 1:30 - 4:30 p.m. |Salon E GTPase Oliver Daumke; Max Delbruck Center for Molecular 1:30 - 1:35 p.m. Introduction from Chair Medicine; Berlin, Germany Hyuntae Na, Penn State Harrisburg; Pennsylvania, United States 2:05 - 2:35 p.m. Expanding Roles for the ESCRT Machinery Phyllis Hanson, Washington University; 1:35 - 2:05 p.m. Targeting Cancer Using Small Molecule Degraders Missouri; United States Nathanael Gray, Harvard University; Massachusetts; United States 2:35 - 2:50 p.m. Protein Science Best Paper Award Winner Becn2 Interacts With Atg14 Through a Metastable 2:05 - 2:35 p.m. Electrophile Fragment Screening as a Rapid Method Coiled-Coil to Mediate Autophagy for Covalent Probe Discovery Minfei Su, Weill Cornell Medical College; Nir London, Weizmann Institute of Science; New York, United States Rehovot, Israel Coffee Break I 2:50 - 3:15 p.m. I Gloucester 2:35 - 2:50 p.m. Massively Parallel Protein Design to Develop Enzymes for Next-Generation Chemotherapy 3:15 - 3:45 p.m. Chaperoning SNARE Assembly to Control Membrane Brahm Yachnin, Rutgers University; Fusion New Jersey, United States Fred Hughson, Princeton University, Princeton, New Jersey; United States Coffee Break | 2:50 - 3:15 p.m. |Gloucester 3:45 - 4 p.m. Structure of the Human TRPM4 Ion Channel in a Lipid 3:15 - 3:45 p.m. Constraining Evolution -- Avoiding Drug Resistance: Nanodisc Lessons from Viruses Henriette Autzen, University of California San Francisco; Celia Schiffer, University of Massachusetts Medical California, United States School; Worcester, Massachusetts; United States 4 - 4:30 p.m. The Initiation of Ubiquitin-Independent Mitophagy by 3:45 - 4 p.m. The Structural Basis for CARD9 and CARD11 Atg32 Autoinhibition Michael Ragusa, Dartmouth College; Michael Holliday, Genentech, California, United States New Hampshire, United States 4 - 4:30 p.m. A Structural Mechanism for Directing Inverse Agonism of PPAR? POSTERS OPEN, EXHIBITS, MIX & MINGLE Douglas Kojetin, The Scripps Research Institute; 4:30 - 6:30 p.m. |Gloucester California, United States Baseball Game (Red Sox vs. Rangers) 7:10 - 10:00 p.m. |Fenway Park

28 29 CONCURRENT MORNING SESSION 6 #PS32 Proteins in the Microbiome and Immune 8:30 - 11:45 a.m. |Salon F DayProgram 2 - Tuesday, July 10, 2018 8:30 - 8:35 a.m. Introduction from Chair 7:15 a.m. - 8:30 a.m. |Exhibitor Workshop Creoptix |Arlington Mikaela Stewart, Texas Christian University; NEW MEMBER WELCOME BREAKFAST/MEMBER BUSINESS MEETING Texas, United States 7:30 - 8:15 a.m. | Berkeley Room 8:35 - 9:05 a.m. LAPS Exchange Speaker CONCURRENT MORNING SESSION 5 Metallo-ß-lactamases: a Tug of War between Bacteria Functional Protein Dynamics and Allostery and the Immune System for the available Zn(II) 8:30 - 11:45 a.m. |Salon E Alejandro Vila, IBR/Universidad Nacional de Rosario, Santa Fe; Argentina 8:30 - 8:35 a.m. Introduction from Chair Mylene Ferrolino, St. Jude Children's Research 9:05 - 9:35 a.m. Structural Biochemistry of Cellular Proteins Usurped by Hospital; Tennessee, United States Viruses Blanton Tolbert, Case Western Reserve University; 8:35 - 9:05 a.m. Ultra-Fast Photoswitching In Fluorescent Proteins Ohio, United States Observed by Time-Resolved Serial Femtosecond Crystallography 9:35 - 9:50 a.m. Interrogating a Multidrug Effl ux Membrane Protein Martin Weik, IBS; France Transporter Involved In Bacterial Antibiotic Resistance Using Structural Mass Spectrometry 9:05 - 9:35 a.m. Improved Physical Models Enable the Investigation Zainab Ahdash, King's College, London, UK of Molecular Recognition in Intrinsically Disordered Proteins at Atomistic Resolution COFFEE BREAK | 9:50 - 10:15 a.m. |Gloucester Paul Robustelli, DE Shaw Research; New York, United States 110:15 - 10:45 a.m. Structure and Mechanism of an Exceptionally Powerful Motor that Powers Virus Assembly 9:35 - 9:50 a.m. Protein Science Best Paper Award Winner Brian Kelch, University of Massachusetts Med School; Single-Molecule Imaging Revealst the Translocation Massachusetts, United States and dna Looping Dynamics of Hepatitis C Virus Ns3 Helicase 10:45 - 11:15 a.m. Weapons to Probes: Using Toxins to Study the Bacterial Chang-Ting Lin, Johns Hopkins University; Cell Wall Maryland, United States Seemay Chou, University of California San Francisco; California, United States COFFEE BREAK | 9:50 - 10:15 a.m. |Gloucester 11:15 - 11:45 a.m. NMR Characterization of Changes in Acid-Stress 10:15 - 10:45 a.m. The Evolution of Dynamic Amino Acid Interaction Bacterial Chaperone HdeA as a Function of pH in Networks Around the Catalytic Cycle of a Preparation for Activation Tryptophan Synthase Karin Crowhurst, California State University Northridge; David Boehr, Pennsylvania State University; California, United States Pennsylvania, United States LUNCH |11:45 a.m. - 1:30 p.m. 10:45 - 11:15 a.m. Allosteric Tuning of Hsp70 Molecular Chaperones Boxed Lunch Pick Up Station |Gloucester Lila Gierasch, U Mass Amherst; Massachusetts, United States 11:45 a.m. - 1:30 p.m. |Exhibitor Workshop Pall ForteBio, LLC |Arlington

11:15 - 11:45 a.m. Simulating the Dynamics of GTPases on the Ribosome 12:15 - 1:30 p.m. |Educators' Panel|St. Botolph Paul Whitford, Northeastern University; 30 Poster Displays & Exhibits Open |Gloucester 31 CONCURRENT AFTERNOON SESSION 8 #PS32 Protein Engineering for Genome Engineering Program 1:30 - 4:30 p.m. |Salon F Day 2 - Tuesday, July 10, 2018 (cont.) 1:30 - 1:35 p.m. Introduction from Chair James Moody, Brigham Young University, CONCURRENT AFTERNOON SESSION 7 Utah, United States Member-Selected Session Repetitive, Non-Globular Proteins: Nature to Nanotechnology 1:35 - 2:05 p.m. Evolutionary Outcomes of CRISPR-anti-CRISPR Confl ict 1:30 - 4:30 p.m. |Salon E Blake Wiendenheft, Montana State University; Montana, United States 1:30 - 1:35 p.m. Introduction from Chair Mary Munson, University of Massachusetts Medical 2:05 - 2:35 p.m. An APOBEC3A-Cas9 Base Editor with Minimized School; Massachusetts, United States Bystander and Off-Target Activities Keith Joung, Massachusetts General Hospital; 1:35 - 2:05 p.m. Repeat Protein Scaffolds for the Design of Functional Massachusetts, United States Nanostructures and Biomaterials Aitziber Cortajarena, BioGune; San Sebastian, Spain 2:35 - 2:50 p.m. Structural Insights into CRISPR and Anti-CRISPR Systems for Precise Genome Editing 2:05 - 2:35 p.m. Protein Materials: From Nature to Nanotechnology Fuguo Jiang, University of California-Berkeley; Tijana Grove, Virginia Tech; Virginia, United States California, United States

2:35 - 2:50 p.m. Collagen Architecture Regulates the Specifi city of Coffee Break I 2:50 - 3:15 p.m. I Gloucester Interactions with its Receptors Cody Hoop, Rutgers University; New Jersey, 3:15 - 3:45 p.m. CRISPR-Cas Mediated Cleavage of Invading Nucleic United States Acids Yanli Wang, Institute of Biophysics, Chinese Academy of Coffee Break I 2:50 - 3:15 p.m. I Gloucester Sciences; Beijing, China

3:15 - 3:45 p.m. Repetitive Proteins On The Surface Of Gram-Positive 3:45 - 4 p.m. Re-Targeting a Bacterial Assassin: Engineering Plyc Bacteria Specifi city Using Directed Evolution Jennifer Potts, University of York, England, UK Sebastian Broendum, Monash University; 3:45 - 4 p.m. Evolution of Environmentally-Enforced, Repeat Protein Melbourne, Australia Topology in the Outer Membrane 4 - 4:30 p.m. LORNE Exchange Speaker Joanna Slusky, University of Kansas; Evolution of an Enzyme from a Solute-Binding Protein Kansas, United States Colin Jackson, Australian National University; 4 - 4:30 p.m. Extensible Protein Scaffolds Based on Beta Solenoids Canbarra, Australia James Murray, Imperial College, London; England, UK POSTER PRESENTATIONS, EXHIBITS, MIX & MINGLE 4:30 - 6:30 p.m. |Gloucester

MENTORING PANEL 6:45 - 7:45 p.m. |Salon E

32 33 #PS32 CONCURRENT MORNING SESSION 10 Multiplexed Protein Science: Deep Mutational Scanning & Program Applications 8:30 - 11:45 a.m. |Salon F Day 3 - Wednesday, July 11, 2018 8:30 - 8:35 a.m. Introduction from Chair CONCURRENT MORNING SESSION 9 Kathryn McMenimen, Mt. Holyoke College; Proteostasis: From Midlife Crisis to the Death of Proteins Massachusetts; United States 8:30 - 11:45 a.m. |Salon E 8:35 - 9:05 a.m. 3D Structure from GeneticVariation 8:30 - 8:35 a.m. Introduction from Chair Deborah Marks, Harvard University; Meghan Breen, University of Michigan; Massachusetts, United States Michigan, United States 9:05 - 9:35 a.m. Using Next Generation Sequencing to Engineer 8:35 - 9:05 a.m. Substrate Processing, Conformational Changes, and Protein-based Therapeutics Mechano-Chemical Coupling of the 26S Proteasome- Christian Cunningham, Genentech, California, a Fine-Tuned Molecular Machine United States Andreas Martin, University of California-Berkeley; California, United States 9:35 - 9:50 a.m. Broad Mutational Scanning Across Protein Families Calin Plesa, UCLA; California, United States 9:05 - 9:35 a.m. The Ups and Downs of Protein Expression Regulation Christine Vogel, New York University; New York, COFFEE BREAK I 9:50 - 10:15 a.m. I Gloucester United States 10:15 - 10:45 a.m. Understanding Protein-Protein Interactions Through 9:35 - 9:50 a.m. The HECT C-terminal Lobe of HERC6 Reveals a Unique Comprehensive Mapping of Binding Landscapes Autoinhibitory Domain Swapping Mechanism Julia Shifman, Hebrew University of Jerusalem; Israel Donald Spratt, Clark University; Massachusetts, United States 10:45 - 11:15 a.m. Using Deep Mutational Scanning to Probe Protein Function, Structure and Regulation COFFEE BREAK I 9:50 - 10:15 a.m. I Gloucester Doug Fowler, University of Washington, Washington, United States 10:15 - 10:45 a.m. Dual Chaperone Function in Nascent Protein Folding Christian Kaiser, Johns Hopkins University; 11:15 - 11:45 a.m. Solving Protein Structure Using Genetics Maryland, United States Jorn Schmiedel, Centre for Genomic Regulation; Barcelona, Spain 10:45 - 11:15 a.m. How the Proteasome Selects its Targets for Destruction Andreas Matouschek, University of Texas, Austin; LUNCH Texas, United States 11:45 a.m. - 1:30 p.m.

11:15 - 11:45 a.m. Structural Biology in Cellular Environments Using High Noon - 1:00 p.m. | Wiley Publisher's Workshop |Arlington Room Sensitivity nmr Kendra Frederick, UT Southwestern; 11:45 a.m.-1:30 p.m. | Exhibitor Workshop - Wyatt Technology Corp. |St. Botolph Texas, United States 11:45 a.m.-1:30 p.m. | Exhibitor Workshop - Nicoya Lifesciences |Berkeley

12:15 - 1:30 p.m. | Undergraduate Research Session |Harvard Room 34 35 Program #PS32 Day 3 - Wednesday, July 11, 2018 (cont.) PLENARY AWARDS SESSION 1:30 - 5:30 p.m. |Salons E & F 3:45 - 3:50 p.m. Presentation of the Emil Thomas Kaiser Award

1:30 - 1:35 p.m. Introduction from The Protein Society President 3:50 - 4:20 p.m. Biological Phase Separation: Mechanisms, Regulation Charles L. Brooks III, University of Michigan and Function 2018 Emil Thomas Kaiser Award Winner 1:35 - 1:40 p.m. Presentation of the Dorothy Crowfoot Hodgkin Award Michael Rosen, University of Texas Southwestern (Sponsored by Genentech) Medical School; Texas, United States

1:40 - 2:10 p.m. Protein Folding - On and Off the Ribosome 4:20 - 4:25 p.m. Presentation of the Protein Science Young Investigator 2018 Dorothy Crowfoot Hodgkin Award Winner Award (Sponsored by Wiley) Susan Marqusee, University of California-Berkeley; California, United States 4:25 - 4:55 p.m. Structural Biology in the Gas Phase: New Techniques for the Rapid Analysis of Protein Sequence, Structure 2:10 - 2:15 p.m. Presentation of the Carl Brändén Award and Stability (Sponsored by Rigaku) Brandon Ruotolo, University of Michigan; Michigan, 2:15 - 2:45 p.m. Exploring the Wilds of Structural Biology: Details, United States

Principles, and Tools 4:55 - 5:05 p.m. Presentation of The Protein Society Service Awards 2018 Carl Brändén Award Winner Jane and Dave Richardson, Duke University; 5:05 - 5:30 p.m. Presentation of Hans Neurath Outstanding Promise North Carolina, United States Travel Awards 2:45 - 2:50 p.m. Presentation of the 2018 Christian B. Anfi nsen Award POSTERS OPEN, EXHIBITS, MIX & MINGLE 2:50 - 3:20 p.m. Single Particle Cryo-EM of Membrane Protein in Lipid 5:30 - 7:30 p.m. |Gloucester Nanodisc Yifan Cheng, University of California San Francisco; MEMBERS' RECEPTION (all welcome) California, United States 8:30 - 10:30 p.m. | Salon F Presentation of the Best Poster Competition Winners COFFEE BREAK I 3:20 - 3:45 p.m. I Gloucester

36 37 Program #PS32 Day 4 - Thursday, July 12, 2018 Day 4 - Thursday, July 12, 2018 (cont.) CONCURRENT MORNING SESSION 11 9:35 - 9:50 a.m. Fluorescent Sensors for Detection of Protein Phase Transitions and Mesoscale Structure Carbonylation 8:30 - 10:35 a.m. |Salon E Kamalika Mukherjee, Massachusetts General Hospital, Harvard University; Massachusetts, United States 8:30 - 8:35 a.m. Introduction from Chair Jamie Towle-Weicksel, Rhode Island College; 9:50 - 10:20 a.m. Genomically Recoded Organisms: Living Foundries for Rhode Island; United States Producing Genetically-Encoded Materials Farren Isaacs, Yale University; 8:35 - 9:05 a.m. Disease Mutations and Post-Translational Modifi cations Connecticut, United States Alter Disordered Protein Liquid-Liquid Phase Separation Nicolas Fawzi, Brown University; COFFEE BREAK | 10:20 - 10:50 a.m. |Foyer Rhode Island, United States CLOSING PLENARY and 2018 STEIN & MOORE AWARD 9:05 - 9:35 a.m. RNA Structure Encodes Specifi city in a PolyQ Protein 10:50 a.m. - 11:45 a.m. Phase Separation Salon E Amy Gladfelter, University of North Carolina; North Carolina, United States 10:50 - 10:55 a.m. Introduction from The Protein Society President and Presentation of the Stein & Moore Award Winner 9:35 - 9:50 a.m. Mechanism and Consequences of Reentrant Phase Charles L Brooks III, University of Michigan Transition of Intrinsically Disordered Proteins Priya Banerjee, University at Buffalo, SUNY; 10:55 - 11:25 a.m. A New Approach Towards Diabetes Drug Discovery New York, United States 2018 Stein & Moore Award Winner Raymond Stevens, University of Southern California; 9:50 - 10:20 a.m. Complex Phenotypic Landscape of a Simple California, United States Phase-Separated Protein System Emmanuel Levy, Weizmann Institute of Science; 11:25 - 11:45 a.m. Closing Remarks from The Protein Society President Rehovot, Israel Charles L. Brooks III, University of Michigan

CONCURRENT MORNING SESSION 12 Beyond 20 Amino Acids: Unnatural Mutagenesis 8:30 - 10:35 a.m. |Salon F

8:30 - 8:35 a.m. Introduction from Chair Denise Okafor, Emory University; Georgia; United States

8:35 - 9:05 a.m. Repurposing Ribosomes for Synthetic Biology Mike Jewett, Northeastern University; Massachusetts, United States

9:05 - 9:35 a.m. The RaPID Way to Discover Bioactive Pseudo-Natural Peptides With Macrocyclic Scaffold Hiroaki Suga, University of Tokyo and Peptidream; 38 Tokyo, Japan 39 Exhibitor Directory #PS32

Beckman Coulter Booth 206

Cell Free Sciences Booth 105

Creoptix Booth 111

Fluidic Analytics Booth 204

Malvern Panalytical Booth 117

NanoTemper Technologies Booth 107

Nicoya Lifesciences Booth 214

NMX Booth 109

Pall ForteBio, LLC Booth 208

PerkinElmer Booth 220

Pressure Bio Sciences, Inc. Booth 116

Redshift BioAnalytics Booth 112

St. Jude Children's Research Hospital Booth 218

TA Instruments Booth 212

Wyatt Technology Corporation Booth 108

The Protein Society/Wiley Booth 114

40 39 #PS32 drug discovery. Engineered around a proprietary waveguide interferometry technolo- Exhibitor Directory gy and a powerful yet intuitive software, the WAVE system offers superior data quality BECKMAN COULTER BOOTH 206 across the broadest range of compounds and sample types. The Creoptix® WAVE 5350 Lakeview Parkway S. Drive accurately characterizes weak binder kinetics with off-rates of 5/sec as well as high af- Indianapolis, Indiana 46268, United States fi nity antibodies with several hours of dissociation. The microfl uidics sustains pure serum, Phone: 800-742-2345 cell supernatant, larger particles and even crude membrane preparations enabling novel approaches especially in the fi eld of membrane protein research. Email: [email protected] Web: www.beckman.com FLUIDIC ANALYTICS Unit 5 Chesterton Mill, French's Road, Beckman Coulter Life Sciences manufactures precision instruments (centrif- BOOTH 204 ugation, analytical ultracentrifugation, automated solutions, particle charac- Cambridge, CB4 3NP, United Kingdom terization, cell counting and viability and research low cytometry) to study Phone: (+44) 01223 560 432 complex biological problems. Our team of experts dedicates the time and Web: https://www.fl uidic.com/ energy to understand the complexity of research for laboratory customers in a wide variety of settings: universities, government, biotechnology and phar- Fluidic Analytics' vision is that protein science will transform our understanding maceutical companies, hospitals, and commercial laboratories. By innovating of how the biological world operates in real time, a transformation every bit new processes and technologies, we’re challenging conventional wisdom; as revolutionary as the one we’ve seen in DNA sequencing. And Fluid- our goal is to develop the best, most widely trusted laboratory solutions ic Analytics aim to make this vision a reality by developing products that available on the market today. enable easier, faster, more convenient and more accurate protein charac- terisation. Our fi rst product – the Fluidity One – measures changes in protein BOOTH 105 CELL FREE SCIENCES size caused by folding, aggregation or interactions in solution in biologically 75-1, Ono-cho, Leading Venture Plaza 201, relevant timescales, without the need for matrices or surfaces and without a bias towards large species. And because measurement is fast and requires as Tsurumi-ku, Yokohama, Kanagawa 230-0046, Japan little as 50 nanograms of protein this makes the Fluidity One perfect for rapid Phone: +81-(0)45-500-2119 | Fax: +81-(0)45-500-2117 quantifi cation and characterisation - from small peptides to large complex- Email: [email protected] es and over a wide range of concentrations. Web: http://www.cfsciences.com/eg/ Web: http://www.cfsciences.com/jp/index.html MALVERN PANALYTICAL CellFree Sciences (CFS) is an ISO9001:2015 certifi ed provider of comprehen- 117 Flanders Road sive solutions for wheat germ cell-free protein production and analysis using Westborough MA 01581, United States the ENDEXT® Technology Platform originally developed in the laboratory of Phone: 508-768-6400 | Fax: 508-768-6403 BOOTH 117 Prof. Yaeta Endo at Ehime University in Japan. With our different WEPRO® Email: [email protected] wheat germ protein expression extracts, CFS is serving the research commu- Web: www.malvern.com nity and customers in industry with protein synthesis services, reagents, and the fully automated Protemist® robotic protein production systems. Malvern Panalytical is a leader in analytical characterization, creating expert solutions for the challenges associated with maximizing productivity, CREOPTIX AG developing better quality products and getting them to market faster. We BOOTH 111 provide superior, customer-focused solutions and services which deliver tangi- Einsiedlerstrasse 34 ble economic impact through chemical, biophysical and structural analysis. CH-8820 Wädenswil, Switzerland Phone: +41 44 533 26 60 [email protected]

Creoptix revolutionizes the study of molecular interactions: By combining best-in- class sensitivity with a crude sample robustness normally only achieved with plate- based assays and a very fast transition capability, the Creoptix® WAVE system is revolutionizing the study of molecular interactions and changing the world of 42 43 PALL FORTEBIO LLC BOOTH 208 47661 Fremont Boulevard #PS32 Fremont, CA 94538, United States Exhibitor Directory Phone: 650-322-1360 | Fax: 650-322-1370 NANOTEMPER TECHNOLOGIES BOOTH 107 400 Oyster Point Blvd, Ste 336 Email: [email protected] South San Francisco, CA 94080, United States Web: www.fortebio.com Phone: 650-763-1658 | Fax: 650-350-4390 Pall ForteBio LLC is one of the world's leading providers of label-free, Email: [email protected] high-throughput and micro-volume analysis solutions for life sciences, bio- Web: www.nanotemper-technologies.com pharmaceutical research, development, and manufacturing. The product portfolio includes instruments, software and biosensors that enable scientists to NanoTemper Technologies is deeply committed to the best customer expe- measure biomolecular interaction kinetics, affi nity, and concentration for their rience. Central to this is a strong focus on enabling researchers to easily, effi - medical and biological research. ciently, and accurately perform protein characterization. With a broad offering of instrumentation, software and consumables for evaluating binding affi nities BOOTH 220 and protein stability, scientists in pharmaceutical, biotech or academic labs PERKINELMER will fi nd an optimized workfl ow, quality results and responsive customer support. 68 Elm Street Work with a deeply experienced and globally operating team, and realize the Hopkinton, MA 01748, United States NanoTemper experience. Phone: 800-762-4000 Email: [email protected] NICOYA LIFESCIENCES BOOTH 214 Web: www.perkinelmer.com 226-283 Duke St W PerkinElmer is a global leader focused on improving the health and Kitchener, Ontario, N2H 3X7, Canada safety of people and the environment. Our dedicated team of 7,700 Phone: 1-877-673-6777 employees worldwide are passionate about providing customers with an Email: [email protected] unmatched experience as they help solve critical issues in human and Web: www.nicoyalife.com environmental health. Our innovative detection, imaging, informatics and service capabilities, combined with deep market knowledge and ex- Nicoya Lifesciences uses nanotechnology to make OpenSPR™, the world’s pertise, help customers gain greater insights into their science to better fi rst benchtop surface plasmon resonance instrument for molecular interaction protect our environment, our food supply and the health of our families. analysis. It is affordable, user-friendly and low maintenance, providing powerful label-free analysis and high quality real-time data for a fraction of the cost PRESSURE BIOSCIENCES, INC. BOOTH 116 of traditional SPR instruments. OpenSPR is perfect for analyzing interactions between proteins, antibodies, nucleic acids and more. With OpenSPR, every 14 Norfold Avenue researcher can now have access to this powerful analysis technique – perfect South Easton, MA 02375 United States of academia, industry, and education. Phone: 508-230-1828 Email: [email protected] Web: www.pressurebiosciences.com NMX BOOTH 109 500 Cartier Blvd W., Ste. 6000 Laval, Québec, Canada H7V 5B7 Pressure BioSciences, Inc (OTCQB: PBIO) is a leader in the development and Phone: 1-514-756-3466 sale of innovative, broadly enabling, pressure-based platform solutions for the life sciences industry. Our products and services are based on the unique properties Email: [email protected] of our patented, pressure-enhanced platforms: Pressure Cycling Technology Web: www.nmxresearch.com ("PCT”) and Pressure Enabled Protein Manufacturing Technology (“PreEMT”). The NMX conducts drug discovery programs via contract research organization PCT Platform is used in biomarker and target discovery, soil and plant biology, and strategic partnership business models. Our ambition is to become a anti-bioterror, and forensics. The GMP-compliant EXT instrument is available to leader not only in the use of NMR spectroscopy tools but also in employing biopharmaceutical drug manufacturers for use in the design, development, molecular biology, biophysic and synthetic chemistry strategies for identifi ca- characterization and quality control of therapeutic proteins. The PreEMT Platform tion of the seeds for tomorrow’s innovative drugs. employs high pressure for the disaggregation and controlled refolding of proteins to their native structures. PreEMT is offered as a service by PBI’s Biological Con- 44 tract Research Services Group. Manufacturing licenses are available. 45 Exhibitor Directory #PS32 REDSHIFT BIO ANALYTICS BOOTH 112 131 Middlesex Turnpike Burlington, MA 01803, United States T: 781.345.7300 E: [email protected] Web: www.redshiftbio.com

RedShiftBio, provider of analytical instrumentation for the R&D and manufacturing of protein drugs, has developed Microfl uidic Modulation Spectroscopy to probe protein biophysical structure. MMS measures stability, similarity, concentration, secondary structure and aggregation in a single automated analysis, with high sensitivity to see change over the widest concentration range without dilution.

ST. JUDE CHILDREN’S RESEARCH HOSPITAL BOOTH 218 262 Danny Thomas Place, MS 276 Memphis, TN, 38105, United States Phone: 901-595-2750 | Fax: 901-595-5376 Email: [email protected] Web: https://www.stjude.org/postdoc

St. Jude is a non-profi t research institution with 240 faculty, where basic research is rapidly translated into groundbreaking treatments for cancer, and other life-threatening diseases. Consistently ranked on FORTUNE magazine's "100 Best Companies to Work For" list. Postdoctoral opportunities are available in a broad range of biomedical and biophysical research areas.

TA INSTRUMENTS BOOTH 212 159 Lukens Drive, New Castle, DE 19720, United States Phone: 302-427-4000 Email: [email protected] Web: www.tainstruments.com

At TA Instruments we believe in offering solutions through quantitative un- derstanding and multi-parameter analysis. By measuring native systems via their heat production, we enable scientists to address both questions of "how stable" and "how fast", two tenets of a chemical system. Our Affi nity ITC and Nano DSC, both with automated options, are high precision calorimeters for label-free measurements of binding interactions, biomolecular structure and stability. We also offer the ultrasensitive TAM IV isothermal calorimeter, a confi gurable platform with applications ranging from shelf-life stability for small molecule and biologics, amorphicity content, microbial activity, and more. Visit us to learn about the very latest in our applications using native assays. 46 47 Exhibitor Directory WYATT TECHNOLOGY CORPORATION BOOTH 108 6330 Hollister Avenue Santa Barbara, CA 93117, United States Phone: 901-595-2750 | Fax: 901-595-5376 Email: [email protected] Web: https://www.stjude.org/postdoc

Wyatt Technology is the recognized leader in instrumentation and software for determining the absolute molar mass, size, charge and interactions of macro- molecules and nanoparticles in solution. These tools include: in-line multi-angle static light scattering– SEC-MALS, high-throughput dynamic light scattering – DLS, high-sensitivity electrophoretic mobility–MP-PALS, fi eld fl ow fractionation –FFF-MALS, automated composition gradients for interaction analysis–CG-MALS, differential refractometry, and differential viscosity. Wyatt's training, service and support are widely considered the industry benchmark of excellence.

WILEY and THE PROTEIN SOCIETY BOOTH 114 111 River Street Hoboken, NJ 07030, United States Phone: 201-748-6000 | Fax: 201-748-6088 Email: [email protected] | Web: www.wiley.com

Wiley is the proud publisher of The Protein Society's fl agship journal, Protein The Protein Society presents Science. They are a global provider of content-enabled solutions to improve seven awards annually to outcomes in research, education, and professional practice with online tools, journals, books, databases, reference works and laboratory protocols. With distinguished scientists. They strengths in every major academic, scientifi c, and professional fi eld, Wiley recognize excellence and proudly partners with over 800 prestigious societies representing 2 million mem- outstanding achievements bers. Download a free Protein Science iPhone, iPad, and Android app at www. in the multidisciplinary fi elds wiley.com. of protein science, and THE PROTEIN SOCIETY and WILEY honor contributions in the areas of leadership, educa- Awards 18336 Soledad Canyon Road, #1217 Stein & Moore Canyon Country, California 91386, United States tion & service. Phone: 844-377-6834 Hans Neurath Email: [email protected] | Web: www.proteinsociety.org We will present the 2019 Dorothy Crowfoot Hodgkin awards at our 33rd Annu- Emil Thomas Kaiser Since 1985, TPS has served as the intellectual home of investigators across all dis- al Symposium in Seattle, Carl Branden ciplines - and from around the world - involved in the study of protein structure,ucture, Christian B. Anfi nsen function, and design. TPS provides forums for scientifi c collaboration andnd com- WA, June 30 - July 3, 2019. Protein Science Young Investigator munication and supports professional growth of young investigators throughhrough Deadline to submit com- workshops, networking opportunities, and by encouraging junior researchersarchers to plete award nomination participate fully in the Annual Symposium. As well as the meeting, the Society’ss packages is noon EDT on prestigious journal Protein Science, edited by Brian Matthews, serves as an ideidealeal platform for furthering the science of proteins in the broadest possible sense.se November 15, 2018. 48 4949 Poster/Abstract #PS32 Schedule Session 1 Monday, July 9, 4:30 - 6:30 p.m. Gloucester Room (All Posters Up) Ϭϰϴ WK^Ϭϱϰ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ d KZη WK^dZη dZ< Ϭϰϵ WK^Ϭϴϳ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ DKEz ϬϬϭ WK^ϭϯϴ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ ϬϱϬ WK^Ϭϴϵ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ :h>zϵ͕ϮϬϭϴ ϬϬϮ WK^ϯϬϮ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ ϰ͗ϯϬWDͲϲ͗ϯϬWD ϬϬϯ WK^ϯϬϯ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϭ WK^ϬϵϬ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϬϬϰ WK^Ϯϳϯ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ ϬϱϮ WK^Ϭϵϱ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϬϬϱ WK^Ϭϱϭ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϯ WK^ϭϬϴ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϬϬϲ WK^Ϭϳϰ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϰ WK^ϭϮϯ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϬϬϳ WK^Ϭϳϲ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϲ WK^ϬϭϮ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϬϴ WK^ϭϬϭ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϳ WK^ϯϬϴ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϬϵ WK^ϭϯϲ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϴ WK^ϬϯϮ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϭϬ WK^ϰϱϮ Ϯ͘ŝŽŝŶĨŽƌŵĂƚŝĐƐ Ϭϱϵ WK^Ϭϯϵ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϭ WK^ϱϬϭ Ϯ͘ŝŽŝŶĨŽƌŵĂƚŝĐƐ ϬϲϬ WK^Ϭϱϵ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϭϮ WK^ϮϬϱ Ϯ͘ŝŽŝŶĨŽƌŵĂƚŝĐƐ Ϭϲϭ WK^Ϯϯϭ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϯ WK^ϮϮϳ Ϯ͘ŝŽŝŶĨŽƌŵĂƚŝĐƐ ϬϲϮ WK^Ϯϯϵ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϱ WK^ϰϲϱ ϯ͘ŚĂƉĞƌŽŶĞƐ Ϭϲϯ WK^ϮϬϴ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϲ WK^ϭϱϯ ϯ͘ŚĂƉĞƌŽŶĞƐ Ϭϲϰ WK^ϭϮϴ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϳ WK^Ϯϰϲ ϯ͘ŚĂƉĞƌŽŶĞƐ Ϭϲϳ WK^Ϭϱϲ ϴ͘ŶnjLJŵŽůŽŐLJ Ϭϭϴ WK^ϰϰϬ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϲϴ WK^ϰϱϯ ϴ͘ŶnjLJŵŽůŽŐLJ Ϭϭϵ WK^Ϭϰϴ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϲϵ WK^Ϭϳϵ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϬ WK^Ϭϲϱ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ ϬϳϬ WK^ϰϱϳ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϭ WK^Ϭϲϲ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϭ WK^Ϭϵϳ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϮ WK^ϭϮϵ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ ϬϳϮ WK^ϭϳϮ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϯ WK^ϰϱϱ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϯ WK^ϭϳϳ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϰ WK^ϭϰϬ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϱ WK^ϯϰϲ ϵ͘ǀŽůƵƚŝŽŶ ϬϮϱ WK^ϰϱϲ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϲ WK^ϭϱϮ ϭϬ͘&ŽůĚŝŶŐ ϬϮϲ WK^ϭϱϬ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϳ WK^ϭϲϳ ϭϬ͘&ŽůĚŝŶŐ ϬϮϳ WK^Ϭϭϳ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϳϴ WK^ϰϴϲ ϭϬ͘&ŽůĚŝŶŐ ϬϮϴ WK^ϬϮϰ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϳϵ WK^Ϭϱϱ ϭϬ͘&ŽůĚŝŶŐ ϬϮϵ WK^ϯϴϲ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ ϬϴϬ WK^Ϭϳϯ ϭϬ͘&ŽůĚŝŶŐ ϬϯϬ WK^ϰϬϵ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ ϬϴϮ WK^Ϭϵϲ ϭϬ͘&ŽůĚŝŶŐ Ϭϯϭ WK^ϰϮϬ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϯ WK^Ϭϰϵ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ ϬϯϮ WK^ϭϮϳ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϰ WK^Ϭϳϱ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϯ WK^ϭϲϮ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϱ WK^Ϭϳϴ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϰ WK^ϭϲϲ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϲ WK^Ϭϴϭ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϱ WK^ϭϴϬ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϴ WK^ϭϭϲ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϲ WK^ϭϵϮ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϵ WK^ϭϳϱ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϳ WK^ϭϵϳ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ ϬϵϬ WK^ϭϳϲ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϴ WK^Ϯϭϵ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϵϭ WK^ϭϳϵ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϵ WK^ϮϮϱ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ ϬϵϮ WK^ϰϰϳ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ ϬϰϬ WK^ϯϲϳ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϯ WK^ϬϳϬ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϭ WK^ϯϲϵ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϰ WK^Ϭϳϭ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ ϬϰϮ WK^Ϭϭϱ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϱ WK^ϭϬϵ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϯ WK^ϯϳϬ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϳ WK^ϭϭϮ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϰ WK^ϬϮϱ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϴ WK^ϭϭϱ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϱ WK^ϯϴϵ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϵ WK^ϭϰϲ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϲ WK^ϬϰϮ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϭϬϬ WK^ϭϱϱ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϳ WK^Ϭϱϯ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϭϬϭ WK^ϭϱϲ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ 50 51 Poster/Abstract #PS32 Schedule Session 1 Monday, July 9, 4:30 - 6:30 p.m. Gloucester Room (All Posters Up) ϭϬϮ WK^ϭϲϯ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ ϭϱϰ WK^ϰϭϴ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϯ WK^ϬϰϬ ϭϯ͘DĞƚĂďŽůŝĐĞŶŐŝŶĞĞƌŝŶŐͬĞŶĞƌŐLJĂƉƉůŝĐĂƚŝŽŶƐ ϭϱϱ WK^ϯϯϵ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϱ WK^Ϭϯϯ ϭϰ͘DŽƚŽƌƐΘŵĂĐŚŝŶĞƐ ϭϱϳ WK^Ϭϵϰ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϲ WK^ϭϬϱ ϭϰ͘DŽƚŽƌƐΘŵĂĐŚŝŶĞƐ ϭϱϴ WK^ϭϬϯ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϳ WK^ϰϯϬ ϭϱ͘WĞƉƚŝĚĞƐ ϭϱϵ WK^ϭϭϬ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϴ WK^Ϭϰϯ ϭϱ͘WĞƉƚŝĚĞƐ ϭϲϬ WK^ϭϮϬ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϵ WK^Ϭϱϴ ϭϱ͘WĞƉƚŝĚĞƐ ϭϲϭ WK^ϭϮϭ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϭϬ WK^ϬϬϯ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϮ WK^ϯϲϯ ϮϮ͘^LJŶƚŚĞƚŝĐďŝŽůŽŐLJ ϭϭϭ WK^ϬϬϰ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϭϮ WK^ϯϲϱ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϯ WK^Ϭϲϭ ϮϮ͘^LJŶƚŚĞƚŝĐďŝŽůŽŐLJ ϭϭϯ WK^ϰϭϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϱ WK^ϰϴϯ ϮϮ͘^LJŶƚŚĞƚŝĐďŝŽůŽŐLJ ϭϭϰ WK^ϰϭϰ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϲ WK^ϰϭϮ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϭϱ WK^ϰϮϮ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϴ WK^ϬϲϬ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϭϲ WK^Ϭϰϰ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϵ WK^ϭϵϬ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϭϳ WK^ϰϮϯ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϬ WK^ϮϬϬ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϭϴ WK^ϬϴϮ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϭ WK^Ϯϱϴ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϭϵ WK^ϭϬϮ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϮ WK^Ϭϭϯ Ϯϱ͘dƌĂŶƐĐƌŝƉƚŝŽŶͬƚƌĂŶƐůĂƚŝŽŶͬƉŽƐƚͲƚƌĂŶƐůĂƚŝŽŶĂůŵŽĚŝĨŝĐĂƚŝŽŶƐ ϭϮϭ WK^ϭϭϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϯ WK^Ϭϰϱ Ϯϱ͘dƌĂŶƐĐƌŝƉƚŝŽŶͬƚƌĂŶƐůĂƚŝŽŶͬƉŽƐƚͲƚƌĂŶƐůĂƚŝŽŶĂůŵŽĚŝĨŝĐĂƚŝŽŶƐ ϭϮϮ WK^ϭϭϳ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϰ WK^ϭϭϰ Ϯϱ͘dƌĂŶƐĐƌŝƉƚŝŽŶͬƚƌĂŶƐůĂƚŝŽŶͬƉŽƐƚͲƚƌĂŶƐůĂƚŝŽŶĂůŵŽĚŝĨŝĐĂƚŝŽŶƐ ϭϮϯ WK^ϭϭϴ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϮϰ WK^ϭϭϵ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϮϱ WK^ϭϮϰ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϮϲ WK^ϭϯϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϮϴ WK^ϭϯϵ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϮϵ WK^ϭϰϯ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϬ WK^ϭϰϱ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϭ WK^ϭϱϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϮ WK^ϭϱϴ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϰ WK^Ϭϴϱ ϭϳ͘WƌŽƚĞŝŶƐŝŶĐĞůůƐ ϭϯϱ WK^ϭϳϴ ϭϳ͘WƌŽƚĞŝŶƐŝŶĐĞůůƐ ϭϯϲ WK^Ϯϭϭ ϭϳ͘WƌŽƚĞŝŶƐŝŶĐĞůůƐ ϭϯϳ WK^ϯϬϱ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϯϴ WK^Ϭϲϯ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϰϬ WK^ϱϭϬ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϰϭ WK^ϭϲϬ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϰϮ WK^ϬϮϬ ϭϵ͘WƌŽƚĞŽƐƚĂƐŝƐĂŶĚƋƵĂůŝƚLJĐŽŶƚƌŽů ϭϰϯ WK^ϭϬϰ ϭϵ͘WƌŽƚĞŽƐƚĂƐŝƐĂŶĚƋƵĂůŝƚLJĐŽŶƚƌŽů ϭϰϰ WK^ϭϰϴ ϭϵ͘WƌŽƚĞŽƐƚĂƐŝƐĂŶĚƋƵĂůŝƚLJĐŽŶƚƌŽů ϭϰϱ WK^ϬϮϭ ϮϬ͘^ŝŶŐůĞŵŽůĞĐƵůĞƐƚƵĚŝĞƐ ϭϰϲ WK^ϰϲϳ ϮϬ͘^ŝŶŐůĞŵŽůĞĐƵůĞƐƚƵĚŝĞƐ ϭϰϳ WK^ϬϬϴ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϰϴ WK^ϬϮϯ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϰϵ WK^ϬϮϳ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϬ WK^ϯϯϮ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϭ WK^ϬϲϮ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϮ WK^Ϭϲϰ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϯ WK^Ϭϲϳ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ 52 53 Poster/Abstract #PS32 Schedule Session 2 Tuesday, July 10, 4:30 - 6:30 p.m. Gloucester Room (All Posters Up) d KZη WK^dZη dZ< Ϭϰϴ WK^Ϯϯϰ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ dh^z ϬϬϭ WK^ϬϬϮ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϰϵ WK^ϮϱϮ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ :h>zϭϬ͕ϮϬϭϴ ϬϬϮ WK^ϭϰϭ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ ϬϱϬ WK^Ϯϴϭ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϰ͗ϯϬWDͲϲ͗ϯϬWD ϬϬϯ WK^ϭϴϴ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϭ WK^ϰϮϵ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϬϬϰ WK^Ϭϯϲ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ ϬϱϮ WK^ϰϯϲ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϬϬϱ WK^Ϯϳϲ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϯ WK^ϰϵϬ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϬϬϲ WK^Ϯϳϴ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϰ WK^ϰϵϭ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϬϬϳ WK^Ϯϴϯ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϱ WK^ϱϬϲ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϬϬϴ WK^ϯϵϯ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϳ WK^ϭϯϳ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϬϵ WK^ϰϴϵ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϴ WK^ϭϳϬ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϭϬ WK^ϱϬϰ Ϯ͘ŝŽŝŶĨŽƌŵĂƚŝĐƐ Ϭϱϵ WK^ϭϴϳ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϭ WK^ϯϴϮ Ϯ͘ŝŽŝŶĨŽƌŵĂƚŝĐƐ ϬϲϬ WK^ϭϭϯ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϭϮ WK^ϰϮϭ Ϯ͘ŝŽŝŶĨŽƌŵĂƚŝĐƐ Ϭϲϭ WK^Ϭϴϯ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϰ WK^Ϯϱϰ ϯ͘ŚĂƉĞƌŽŶĞƐ ϬϲϮ WK^Ϯϯϱ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϱ WK^Ϯϳϱ ϯ͘ŚĂƉĞƌŽŶĞƐ Ϭϲϯ WK^ϯϭϯ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϲ WK^ϯϰϮ ϯ͘ŚĂƉĞƌŽŶĞƐ Ϭϲϰ WK^Ϭϵϵ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϳ WK^ϭϱϰ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϲϱ WK^ϰϯϴ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϴ WK^ϭϱϵ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϲϲ WK^ϰϵϯ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ Ϭϭϵ WK^ϭϲϴ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϲϳ WK^Ϯϳϭ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϮϬ WK^ϭϵϱ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϲϴ WK^ϭϵϲ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϭ WK^ϮϮϮ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϲϵ WK^Ϯϴϲ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϮ WK^ϰϳϱ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ ϬϳϬ WK^Ϯϴϵ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϯ WK^ϱϬϬ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϭ WK^ϯϱϰ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϰ WK^ϱϬϯ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ ϬϳϮ WK^ϰϬϱ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϱ WK^ϰϭϯ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϯ WK^ϰϱϵ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϲ WK^ϰϮϱ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϱ WK^ϰϳϬ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϳ WK^ϮϯϬ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϳϲ WK^ϰϵϳ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϴ WK^ϮϰϬ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϳϳ WK^ϰϯϳ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϵ WK^Ϯϰϴ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϳϴ WK^ϰϰϰ ϵ͘ǀŽůƵƚŝŽŶ ϬϯϬ WK^Ϯϱϲ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϳϵ WK^ϯϮϱ ϭϬ͘&ŽůĚŝŶŐ Ϭϯϭ WK^Ϯϴϰ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ ϬϴϬ WK^ϰϱϭ ϭϬ͘&ŽůĚŝŶŐ ϬϯϮ WK^Ϯϴϱ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϭ WK^ϭϴϲ ϭϬ͘&ŽůĚŝŶŐ Ϭϯϯ WK^ϯϮϲ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ ϬϴϮ WK^ϭϵϰ ϭϬ͘&ŽůĚŝŶŐ Ϭϯϰ WK^ϯϯϬ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϯ WK^Ϯϲϱ ϭϬ͘&ŽůĚŝŶŐ Ϭϯϱ WK^ϯϯϭ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϰ WK^Ϯϵϴ ϭϬ͘&ŽůĚŝŶŐ Ϭϯϲ WK^ϯϰϭ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϱ WK^ϯϬϭ ϭϬ͘&ŽůĚŝŶŐ Ϭϯϳ WK^ϰϰϵ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϴ WK^ϭϴϯ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϴ WK^ϰϳϮ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϵ WK^ϭϵϯ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϵ WK^ϱϬϱ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ ϬϵϬ WK^ϭϵϴ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ ϬϰϬ WK^ϱϬϴ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϵϭ WK^ϭϵϵ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϰϭ WK^ϭϮϲ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϬϵϮ WK^ϮϬϯ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ ϬϰϮ WK^ϭϯϰ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϯ WK^ϮϬϳ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϰϯ WK^ϭϰϳ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϱ WK^ϭϳϯ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϰ WK^ϭϱϳ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϲ WK^ϮϬϲ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϱ WK^ϭϲϱ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϳ WK^ϯϵϰ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϲ WK^ϮϮϬ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϴ WK^ϮϮϲ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϳ WK^ϮϮϭ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϵ WK^ϮϯϮ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ 54 55 Poster/Abstract #PS32 Schedule Session 2 Tuesday, July 10, 4:30 - 6:30 p.m. Gloucester Room (All Posters Up) ϭϬϬ WK^Ϯϰϰ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ ϭϰϵ WK^ϰϴϱ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϮ WK^ϰϬϳ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ ϭϱϬ WK^ϱϬϳ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϯ WK^ϮϴϬ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ ϭϱϭ WK^Ϯϱϳ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϰ WK^ϰϮϲ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ ϭϱϮ WK^ϯϭϭ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϲ WK^ϭϴϰ ϭϰ͘DŽƚŽƌƐΘŵĂĐŚŝŶĞƐ ϭϱϯ WK^ϯϭϰ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϳ WK^Ϯϰϵ ϭϰ͘DŽƚŽƌƐΘŵĂĐŚŝŶĞƐ ϭϱϱ WK^ϰϰϴ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϴ WK^Ϯϱϯ ϭϰ͘DŽƚŽƌƐΘŵĂĐŚŝŶĞƐ ϭϱϲ WK^ϯϲϭ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϵ WK^Ϭϲϵ ϭϱ͘WĞƉƚŝĚĞƐ ϭϱϳ WK^ϰϱϬ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϭϬ WK^Ϭϵϴ ϭϱ͘WĞƉƚŝĚĞƐ ϭϱϴ WK^ϯϳϰ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϭϭ WK^ϭϲϵ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϱϵ WK^ϯϳϴ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϭϮ WK^ϭϳϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϬ WK^ϯϴϴ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϭϯ WK^ϭϳϰ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϭ WK^ϯϵϱ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϭϰ WK^ϮϬϮ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϮ WK^ϯϵϴ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϭϱ WK^ϮϭϬ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϯ WK^ϰϭϳ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϭϲ WK^ϰϰϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϰ WK^ϮϲϬ ϮϮ͘^LJŶƚŚĞƚŝĐďŝŽůŽŐLJ ϭϭϳ WK^ϰϲϴ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϰ WK^ϭϯϱ ϮϮ͘^LJŶƚŚĞƚŝĐďŝŽůŽŐLJ ϭϭϴ WK^ϰϲϵ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϱ WK^Ϯϲϰ ϮϮ͘^LJŶƚŚĞƚŝĐďŝŽůŽŐLJ ϭϭϵ WK^ϰϳϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϲ WK^ϯϬϬ ϮϮ͘^LJŶƚŚĞƚŝĐďŝŽůŽŐLJ ϭϮϬ WK^ϰϵϱ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϳ WK^Ϯϲϳ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϮϭ WK^Ϯϯϳ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϴ WK^ϯϭϮ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϮϮ WK^Ϯϯϴ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϵ WK^ϯϰϯ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϮϯ WK^Ϯϰϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϬ WK^ϰϰϲ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϮϰ WK^Ϯϱϵ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϭ WK^ϰϬϬ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϮϱ WK^ϮϲϮ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϯ WK^Ϯϰϳ Ϯϱ͘dƌĂŶƐĐƌŝƉƚŝŽŶͬƚƌĂŶƐůĂƚŝŽŶͬƉŽƐƚͲƚƌĂŶƐůĂƚŝŽŶĂůŵŽĚŝĨŝĐĂƚŝŽŶƐ ϭϮϲ WK^Ϯϲϯ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϮϳ WK^Ϯϲϲ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϰ WK^ϮϬϭ Ϯϱ͘dƌĂŶƐĐƌŝƉƚŝŽŶͬƚƌĂŶƐůĂƚŝŽŶͬƉŽƐƚͲƚƌĂŶƐůĂƚŝŽŶĂůŵŽĚŝĨŝĐĂƚŝŽŶƐ ϭϮϴ WK^Ϯϳϵ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϮϵ WK^Ϯϵϲ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϬ WK^ϯϬϰ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϭ WK^ϯϭϴ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϮ WK^ϯϰϬ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϯ WK^ϯϱϯ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϰ WK^ϯϱϲ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϰ WK^ϭϯϮ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϱ WK^Ϯϯϯ ϭϳ͘WƌŽƚĞŝŶƐŝŶĐĞůůƐ ϭϯϲ WK^ϮϴϮ ϭϳ͘WƌŽƚĞŝŶƐŝŶĐĞůůƐ ϭϯϳ WK^ϮϵϮ ϭϳ͘WƌŽƚĞŝŶƐŝŶĐĞůůƐ ϭϯϵ WK^ϯϭϱ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϰϬ WK^ϯϵϲ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϰϭ WK^Ϯϭϯ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϰϮ WK^Ϯϰϱ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϰϯ WK^ϮϳϬ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϰϰ WK^Ϯϲϵ ϭϵ͘WƌŽƚĞŽƐƚĂƐŝƐĂŶĚƋƵĂůŝƚLJĐŽŶƚƌŽů ϭϰϱ WK^Ϯϳϳ ϭϵ͘WƌŽƚĞŽƐƚĂƐŝƐĂŶĚƋƵĂůŝƚLJĐŽŶƚƌŽů ϭϰϲ WK^ϰϯϭ ϮϬ͘^ŝŶŐůĞŵŽůĞĐƵůĞƐƚƵĚŝĞƐ ϭϰϳ WK^ϰϲϲ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϰϴ WK^ϰϳϰ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ 56 57 Poster/Abstract #PS32 Schedule Session 3 Wednesday, July 11, 5:30 - 7:30 p.m. Gloucester Room (All Posters Up) Ϭϱϯ WK^ϯϱϳ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ d KZη WK^dZη dZ< Ϭϱϰ WK^ϯϬϳ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ tE^z ϬϬϭ WK^Ϭϭϴ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϱ WK^Ϭϭϵ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ :h>zϭϭ͕ϮϬϭϴ ϬϬϮ WK^Ϭϯϱ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϴ WK^ϯϯϰ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϱ͗ϯϬWDͲϳ͗ϯϬWD ϬϬϯ WK^ϯϮϭ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϱϵ WK^ϯϰϰ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϬϰ WK^ϯϱϮ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ ϬϲϬ WK^Ϯϲϭ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϬϱ WK^ϯϵϬ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ ϬϬϲ WK^Ϯϴϳ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϲϭ WK^ϰϰϯ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϬϳ WK^ϰϬϴ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ ϬϲϮ WK^ϰϴϰ ϳ͘LJŶĂŵŝĐƐĂŶĚĂůůŽƐƚĞƌLJ ϬϬϴ WK^ϰϲϯ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϲϱ WK^ϰϯϵ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϬϵ WK^ϮϵϬ ϭ͘ŵLJůŽŝĚĂŶĚĂŐŐƌĞŐĂƚŝŽŶ Ϭϲϲ WK^ϰϰϮ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϭϬ WK^ϬϵϮ Ϯ͘ŝŽŝŶĨŽƌŵĂƚŝĐƐ Ϭϲϳ WK^ϬϳϮ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϭϮ WK^Ϯϵϳ Ϯ͘ŝŽŝŶĨŽƌŵĂƚŝĐƐ Ϭϲϴ WK^ϰϱϰ ϴ͘ŶnjLJŵŽůŽŐLJ Ϭϭϱ WK^ϬϮϮ ϯ͘ŚĂƉĞƌŽŶĞƐ Ϭϲϵ WK^Ϭϵϭ ϴ͘ŶnjLJŵŽůŽŐLJ Ϭϭϲ WK^ϰϳϴ ϯ͘ŚĂƉĞƌŽŶĞƐ ϬϳϬ WK^ϰϱϴ ϴ͘ŶnjLJŵŽůŽŐLJ Ϭϭϴ WK^ϭϯϯ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϭ WK^ϰϭϵ ϴ͘ŶnjLJŵŽůŽŐLJ Ϭϭϵ WK^ϭϰϮ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ ϬϳϮ WK^ϰϮϳ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϬ WK^ϰϲϬ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϯ WK^ϰϮϴ ϴ͘ŶnjLJŵŽůŽŐLJ ϬϮϭ WK^ϯϮϰ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϱ WK^ϮϬϵ ϵ͘ǀŽůƵƚŝŽŶ ϬϮϮ WK^ϰϳϵ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϲ WK^ϯϭϬ ϭϬ͘&ŽůĚŝŶŐ ϬϮϯ WK^ϰϴϬ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϳ WK^ϱϭϭ ϭϬ͘&ŽůĚŝŶŐ ϬϮϰ WK^ϯϮϳ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϴ WK^ϯϰϱ ϭϬ͘&ŽůĚŝŶŐ ϬϮϱ WK^ϯϲϲ ϰ͘ŚĞŵŝĐĂůďŝŽůŽŐLJ Ϭϳϵ WK^ϯϵϳ ϭϬ͘&ŽůĚŝŶŐ ϬϮϲ WK^ϯϳϭ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ ϬϴϬ WK^ϬϬϵ ϭϬ͘&ŽůĚŝŶŐ ϬϮϳ WK^Ϭϳϳ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϭ WK^ϰϲϰ ϭϬ͘&ŽůĚŝŶŐ ϬϮϴ WK^ϯϵϵ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ ϬϴϮ WK^Ϭϰϭ ϭϬ͘&ŽůĚŝŶŐ ϬϮϵ WK^ϰϬϮ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϯ WK^Ϯϭϲ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ ϬϯϬ WK^ϰϬϯ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϰ WK^Ϯϭϴ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϭ WK^ϭϬϳ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϱ WK^ϮϮϯ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϯ WK^ϰϯϯ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϳ WK^ϮϮϵ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϰ WK^ϯϱϬ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϴ WK^ϯϲϮ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϱ WK^ϯϱϴ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϴϵ WK^ϯϳϱ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϲ WK^ϰϵϮ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ ϬϵϬ WK^ϰϬϲ ϭϭ͘/ŶƚƌŝŶƐŝĐĂůůLJĚŝƐŽƌĚĞƌĞĚƉƌŽƚĞŝŶƐ Ϭϯϳ WK^ϯϱϵ ϱ͘ŽŵƉƵƚĂƚŝŽŶĂůŵŽĚĞůŝŶŐͬƐŝŵƵůĂƚŝŽŶ Ϭϵϭ WK^ϯϭϲ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϯϴ WK^ϬϭϬ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϬϵϮ WK^ϯϮϮ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϯϵ WK^Ϭϭϰ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϰ WK^ϯϯϲ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ ϬϰϬ WK^Ϭϭϲ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϲ WK^Ϯϭϰ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϭ WK^ϯϳϵ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϳ WK^Ϯϳϰ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ ϬϰϮ WK^ϯϴϳ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϴ WK^Ϯϴϴ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϯ WK^Ϭϯϴ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ Ϭϵϵ WK^Ϭϲϴ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϰ WK^ϯϮϬ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϭϬϬ WK^ϰϴϴ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϱ WK^ϯϯϯ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϭϬϭ WK^ϰϵϲ ϭϮ͘DĞŵďƌĂŶĞƉƌŽƚĞŝŶƐ Ϭϰϲ WK^ϰϰϱ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϭϬϯ WK^ϯϬϵ ϭϰ͘DŽƚŽƌƐΘŵĂĐŚŝŶĞƐ Ϭϰϳ WK^ϰϳϳ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϭϬϰ WK^ϯϴϭ ϭϰ͘DŽƚŽƌƐΘŵĂĐŚŝŶĞƐ Ϭϰϴ WK^ϰϴϭ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϭϬϱ WK^ϮϮϰ ϭϱ͘WĞƉƚŝĚĞƐ Ϭϰϵ WK^ϰϴϳ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϭϬϲ WK^ϰϭϱ ϭϱ͘WĞƉƚŝĚĞƐ ϬϱϬ WK^ϯϯϱ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϭϬϳ WK^ϬϮϵ ϭϱ͘WĞƉƚŝĚĞƐ Ϭϱϭ WK^ϯϱϱ ϲ͘ĞƐŝŐŶͬĞŶŐŝŶĞĞƌŝŶŐ ϭϬϴ WK^Ϯϵϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ 58 59 Poster/Abstract #PS32 Schedule Session 3 Wednesday, July 11, 5:30 - 7:30 p.m. Gloucester Room (All Posters Up) ϭϭϮ WK^ϯϭϳ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϱϵ WK^Ϯϰϯ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϬϵ WK^ϯϰϳ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϬ WK^Ϯϱϭ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϭϬ WK^ϯϰϵ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϭ WK^Ϭϯϰ ϮϮ͘^LJŶƚŚĞƚŝĐďŝŽůŽŐLJ ϭϭϭ WK^ϯϱϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϮ WK^ϰϬϭ ϮϮ͘^LJŶƚŚĞƚŝĐďŝŽůŽŐLJ ϭϭϰ WK^ϯϲϬ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϭϱ WK^ϭϲϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϯ WK^ϮϬϰ ϮϮ͘^LJŶƚŚĞƚŝĐďŝŽůŽŐLJ ϭϭϲ WK^ϯϲϴ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϰ WK^Ϯϱϱ Ϯϯ͘^LJƐƚĞŵƐďŝŽůŽŐLJ ϭϭϳ WK^ϯϴϬ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϲ WK^ϰϬϰ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϭϴ WK^ϯϴϯ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϴ WK^ϰϭϲ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϭϵ WK^ϬϯϬ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϲϵ WK^ϯϵϮ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϮϬ WK^Ϭϯϭ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϬ WK^ϰϴϮ Ϯϰ͘dŚĞƌĂƉĞƵƚŝĐƐĂŶĚĂŶƚŝďŽĚŝĞƐ ϭϮϭ WK^Ϭϯϳ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϭ WK^ϮϰϮ Ϯϱ͘dƌĂŶƐĐƌŝƉƚŝŽŶͬƚƌĂŶƐůĂƚŝŽŶͬƉŽƐƚͲƚƌĂŶƐůĂƚŝŽŶĂůŵŽĚŝĨŝĐĂƚŝŽŶƐ ϭϮϮ WK^ϬϱϮ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϮ WK^ϭϴϱ Ϯϱ͘dƌĂŶƐĐƌŝƉƚŝŽŶͬƚƌĂŶƐůĂƚŝŽŶͬƉŽƐƚͲƚƌĂŶƐůĂƚŝŽŶĂůŵŽĚŝĨŝĐĂƚŝŽŶƐ ϭϮϯ WK^ϰϮϰ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϯ WK^ϮϱϬ Ϯϱ͘dƌĂŶƐĐƌŝƉƚŝŽŶͬƚƌĂŶƐůĂƚŝŽŶͬƉŽƐƚͲƚƌĂŶƐůĂƚŝŽŶĂůŵŽĚŝĨŝĐĂƚŝŽŶƐ ϭϮϰ WK^ϰϯϮ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϮϱ WK^ϰϯϱ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϳϰ WK^ϯϳϲ Ϯϲ͘KƚŚĞƌ ϭϮϳ WK^ϮϭϮ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϮϴ WK^Ϯϭϱ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϮϵ WK^Ϯϭϳ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϬ WK^ϮϮϴ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϭ WK^ϰϵϰ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϮ WK^Ϯϯϲ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϯ WK^ϱϬϮ ϭϲ͘WƌŽƚĞŝŶŝŶƚĞƌĂĐƚŝŽŶƐĂŶĚĂƐƐĞŵďůŝĞƐ ϭϯϰ WK^Ϯϵϱ ϭϳ͘WƌŽƚĞŝŶƐŝŶĐĞůůƐ ϭϯϱ WK^ϯϮϯ ϭϳ͘WƌŽƚĞŝŶƐŝŶĐĞůůƐ ϭϯϲ WK^ϯϮϵ ϭϳ͘WƌŽƚĞŝŶƐŝŶĐĞůůƐ ϭϯϳ WK^ϬϮϲ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϯϵ WK^ϯϲϰ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϰϬ WK^ϭϴϮ ϭϴ͘WƌŽƚĞŽŵŝĐƐ ϭϰϭ WK^ϯϯϳ ϭϵ͘WƌŽƚĞŽƐƚĂƐŝƐĂŶĚƋƵĂůŝƚLJĐŽŶƚƌŽů ϭϰϮ WK^ϯϰϴ ϭϵ͘WƌŽƚĞŽƐƚĂƐŝƐĂŶĚƋƵĂůŝƚLJĐŽŶƚƌŽů ϭϰϯ WK^ϯϳϮ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϰϰ WK^ϯϳϯ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϰϲ WK^ϯϳϳ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϰϳ WK^ϯϴϰ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϰϴ WK^ϯϴϱ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϰϱ WK^ϯϵϭ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϰϵ WK^ϰϭϬ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϬ WK^ϬϴϬ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϭ WK^ϰϯϰ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϮ WK^Ϭϴϰ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϯ WK^Ϭϱϳ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϰ WK^ϰϲϭ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϱ WK^ϭϮϮ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϲ WK^ϰϳϯ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϳ WK^ϭϴϵ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ ϭϱϴ WK^ϰϳϲ Ϯϭ͘^ƚƌƵĐƚƵƌĞ;džͲƌĂLJͬEDZͬDͿ 60 61 #PS32

members' reception ALL WELCOME July 11, 8:30 - 10:30 p.m. Salon F

53 #PS32 continue to advance so to will the utility of NMR. If anything, NMR is far more valuable today than it was even a decade ago. This will be emphasized through Abstracts a number of examples. TPS Award Winners & Speakers PROTEIN FOLDING - ON AND OFF THE RIBOSOME Susan Marqusee - 2018 Dorothy Crowfoot Hodgkin Award Winner SINGLE PARTICLE CRYO-EM OF MEMBRANE PROTEIN IN LIPID NANODISC University of California, Berkeley Yifan Cheng - 2018 Christian B. Anfi nsen Award Winner HHMI/Biochemistry and Biophysics, UCSF Understanding the structural and dynamic information encoded in the primary sequence of a protein is one of the most fundamental challenges in modern In the last few years, major technological advancements, particularly the de- biology. The amino acid sequence of a protein encodes more than the native velopment of new direct electron detection cameras and associated tech- three-dimensional structure; it encodes the entire energy landscape – an ensem- nologies, have enabled single particle electron cryo-microscopy (cryo-EM) to ble of conformations whose energetics and dynamics are fi nely tuned for folding, become the technique of choice for high-resolution structure determination of binding and activity. Small variations in the sequence and environment modulate many challenging biological macromolecules. We pioneered some of the tech- this landscape and can have effects that range from undetectable to patholog- nologies now being routinely used and applied them to determine atomic struc- ical. I will present our recent results probing these sequence and environmental tures of a number of integral membrane proteins, such as some major members effects using a combination of single-molecule and ensemble-based studies. of transient receptor potential (TRP) channel superfamily. Some of our studies paved the way of applying this method to a wide range of integral membrane I will address a fundamental question in protein folding of whether proteins fold proteins. Nowadays, atomic structures of membrane proteins that are refractory through one or multiple trajectories. By using a combination of chemical denatur- to crystallization are being determined by this method in a rapid pace. ant, mechanical force and site-directed mutations, we can detect the presence of multiple unfolding pathways in a simple, two-state folding protein; the dominant Technologically, we further aimed to enable high-resolution structural studies of pathway can be altered by small changes in the sequence or environment. I will membrane proteins in near native lipid bilayer environment. To this end, we pio- explore the implications of this result for 1) protein folding in complex environments, neered a number of approaches, including reconstituting membrane protein into such as on the ribosome, and 2) the suggestion that evolution can modulate both lipid nanodisc or into saposin based lipid nanoparticles, and developed methodol- the rates of folding and the specifi c pathway. ogy of using conformational specifi c monoclonal Fab or other designed scaf- foldings to facilitate image alignment of very small integral membrane proteins EXPLORING THE WILDS OF STRUCTURAL BIOLOGY: DETAILS, PRINCIPLES, & TOOLS reconstituted into lipid nanoparticles. In a number of recent studies, we observed David Richardson & Jane Richardson - 2018 Carl Brand Award Winners specifi c lipid-protein interactions that play critical role in regulating the channel Duke University functions. In TRPV1 ion channel, as an example, certain specifi c lipid-protein inter- actions enhance binding of a spider toxin to the channel through formation of a We will illustrate a selection of our favorite highlights and anecdotes from the toxin-lipid-TRPV1 tripartite complex, and an endogenous phosphatidylinositol lipid history of our long and varied careers in structural biology, ending with a look at occupies the capsaicin-binding site of the channel. These observations provide the new directions we're excited about right now. important clues about physiological mechanisms of channel regulation. STRUCTURAL BIOLOGY IN THE GAS PHASE: NEW TECHNIQUES FOR THE RAPID SOLUTION NMR: WHY BOTHER? ANALYSIS OF PROTEIN SEQUENCE, STRUCTURE AND STABILITY Lewis Kay - 2017 Christian B. Anfi nsen Award Winner Brandon Ruotolo - 2018 Protein Science Young Investigator Award Winner University of Toronto University of Michigan With the ever-evolving development of new biophysical tools and increasingly Within each living organism proteins are at work, carrying out activities which impact powerful techniques for biomolecular structural studies it is reasonable to con- every aspect of cellular function from synthesis to cell death. The next generation of template the role of solution-based NMR spectroscopy in going forward. In this medicines will rely heavily upon our ability to quickly assess the structures and stabil- talk I will describe a number of studies on molecular machines from my labora- ities of such complex macromolecular machines, as well as the infl uence of large tory, emphasizing the unique role that NMR can play in providing quantitative libraries of conformationally-selective small molecule binders and protein-based descriptions of molecular dynamics and how such motion relates to function. biotherapeutics. Such endeavors are nearly insurmountable with current tools. In this The complementarity of NMR to other structural techniques is such that as they presentation, I will discuss recent developments surrounding the activation of gas- 64 65 #PS32 interface residues to more ideal pairs improves homodimer self-association and Abstracts thermal stability. Unlike BECN1, all BECN2 CCD mutants bind ATG14, although more weakly than wild type. Thus, polar BECN2 CCD interface residues result in a TPS Award Winners & Speakers metastable homodimer, facilitating dissociation, but enable better interactions with polar ATG14 residues stabilizing the BECN2:ATG14 heterodimer. These struc- ture-based mechanistic differences in BECN1 and BECN2 homodimerization and phase protein complex ions aimed at bridging this gap in basic technology. One heterodimerization likely dictate competitive ATG14 recruitment. such development is collision induced unfolding (CIU), which uses ion mobility-mass spectrometry (IM-MS) to measure the stability and unfolding pathways of gas-phase proteins, without the need for covalent labels or tagging, and consuming 10-100 SINGLE-MOLECULE IMAGING REVEALS THETRANSLOCATION AND DNA times less sample than almost any other label-free technology. In parallel with LOOPING DYNAMICSOF HEPATITIS C VIRUS NS3 HELICASE this approach, my lab is pursuing chemical modifi cation strategies aimed at the Chang-Ting Lin (1) - 2018 Protein Science Best Paper Award Winner improved liberation of sequence informative peptide fragments from intact protein Felix Tritschler, Kyung Suk Lee, Meigang Gu, Charles M. Rice, Taekjip Ha, complex precursor ions during collision induced dissociation (CID), enabling the Thomas C. Jenkins assessment of protein quaternary structure and sequence simultaneously. Recent Johns Hopkins University, Baltimore developments in understanding the mechanisms of protein CIU and CID, the ability of these tools to differentiate therapeutic antibodies and enable the discovery of Non-structural protein 3 (NS3) is an essential enzyme and a therapeutic target conformationally-selective inhibitors, will be discussed. of hepatitisC virus (HCV). Compared to NS3-catalyzed nucleic acids unwind- ing, its translation on singlestranded nucleic acids have received relatively little A NEW APPROACH TOWARDS DIABETES DRUG DISCOVERY attention. To investigate the NS3h translocation with single-stranded nucleic Raymond Stevens - 2018 Stein & Moore Award Winner acids substrates directly, we have applied a hybrid platform of single-mole- iHuman Institute, ShanghaiTech University and Bridge Institute, University of cule fl uorescence detection combined with optical trapping. With the aid Southern California of mechanical manipulation and fl uorescence localization, we probed the translocase activity of NS3h on laterally stretched, kilobase-size single-strand- A key scientifi c challenge in biology and chemistry is the integration of data across ed DNA and RNA. We observed that the translocation rate ofNS3h on ssDNA the different scales – molecular, cellular, and whole body. In a collaborative effort at a rate of 24.4 nucleotides per second, and NS3h translocates about three with several different groups across California and Shanghai, we are workings times faster on ssRNA, 74 nucleotides per second. The translocation speed was towards a multi-scale model of the human pancreatic beta cell at atomic resolu- minimally affected by the applied force. A subpopulation of NS3h underwent tion. Such a model will be useful for advancing the fi eld of structure-based drug a novel translocation mode on ssDNA where the stretched DNA shortened design from the protein scale to the cellular scale and provide us with better feed- gradually and then recovers its original length abruptly before repeating the back in the understanding and design of new medicines to treat type II diabetes. cycle repetitively. The speed of this mode of translocation was reduced with increasing force. With corroborating data from single-molecule fl uorescence resonance energy transfer(smFRET) experiments, we proposed that NS3h can BECN2 INTERACTS WITH ATG14 THROUGH A METASTABLE COILED-COIL TO cause repetitive looping of DNA. The smFRETdwell time analysis showed similar MEDIATE AUTOPHAGY translocation time between sole translocation mode versus repetitive looping Minfei Su (1) - 2018 Protein Science Best Paper Award Winner mode, suggesting that the motor domain exhibits indistinguishable enzymatic Yue Li, Shane Wyborny, David Neau, Srinivas Chakravarthy, Beth Levine, activities between the two translocation modes. We propose a potential sec- Christopher L. Colbert, Sangita C. Sinha* ondary nucleic acids binding site at NS3h which might function as an anchor North Dakota State University point for translocation-coupled looping.

ATG14 binding to BECN homologs is essential for autophagy, a critical catabolic homeostasis pathway that is conserved throughout the eukaryotes. We found that the a-helical, coiled-coil domain (CCD) of BECN2, a recently identifi ed mammalian BECN1 paralog, forms an antiparallel, curved homodimer with seven pairs of nonideal packing interactions, while the BECN2 CCD and ATG14 CCD form a parallel, curved heterodimer stabilized by multiple, conserved polar interactions. Compared to BECN1, the BECN2 CCD forms a weaker homod- imer, but binds more tightly to the ATG14 CCD. Mutation of nonideal BECN2 66 67 multiple protein-based hybrid functional nanostructures and biomaterials. #PS32 Among other applications we work on the use of designed proteins as building Abstracts blocks to template:

TPS Award Winners & Speakers (1) Photoactive molecules, in a defi ned distance and orientation that lead to an improvement in the optoelectronic properties. In addition, the unique self Following is the list of invited speakers, denoted by (1), listed alphabetically. assembly properties of CTPR scaffolds have been exploited to generate ordered conductive fi lms of the protein-porphyrin conjugates.[1] WEAPONS TO PROBES: USING TOXINS TO STUDY THE BACTERIAL CELL WALL (2) Carbon nanomaterials, using proteins as wrapping agents for carbon nano- Seemay Chou (1), Atanas Radkov, Jean-Pierre Simorre, Lea Starita, tubes (CNTs) in order to form stable protein-CNTs conjugates.[2] Waldemar Vollmer (3) Electroactive clusters, designing protein scaffolds to coordinate redox active (1) University of California metallic FeS clusters to mimic the redox centers and chains of natural proteins. (4) Gold nanomaterials, using designed and natural fi bril proteins to conjugated The bacterial cell wall is a crosslinked network of glycans and peptides that pro- gold nanoparticles and nanorods for nanometer-precise arrangement of the vides critical structure and support for bacterial cells. This three-dimensional, mesh- nanomaterials.[3] like layer is chemically unique to bacteria, making it a key cellular target for many (5) Fluorescent nanoclusters, by specifi c design of metal coordination sites. As antibiotics and natural antibacterial toxins. For example, bacteria encode diverse a proof of concept, a repeated module with specifi c binding capabilities has lytic, cell wall-degrading enzymes that are delivered against rival neighboring been successfully used to stabilize nanoclusters and applied as a sensor.[4] microbes as a means for competition. Although the cell wall is also an important References surface, studying its interactions with antibacterial proteins has been challenging 1. Mejías, S. H., et al., Chem. Sci. 2016, 7, 4842. given that its composition and organization can vary according to species or 2. López-Andarias, J., et al., Adv. Funct. Materials 2017. Doi: environment. Furthermore, proteins interface with the cell wall as a complex, solid 10.1002/adfm.201704031. substrate. New experimental strategies are needed to build a comprehensive 3. Mejias, S. H., et al., Colloids & Surfaces B: Biointerfaces 2016, 141, molecular model of how the cell wall is recognized and targeted in vivo. We are 93. developing methods to investigate how context-dependent differences in cell 4. Couleaud, P., et al., Biomacromolecules 2015, 16, 3836. walls are effectively and specifi cally sensed by a superfamily of cell wall-targeting toxins deployed in interbacterial competition. By combining traditional structural approaches with a high through-put genetic screening strategy known as deep USING NEXT GENERATION SEQUENCING TO ENGINEER PROTEIN-BASED mutational scanning, our work aims to provide insight into the key determinants THERAPEUTICS governing recognition and breakdown of this critical bacterial surface. Chistian Cunningham (1) (1) Genentech, Inc.

REPEAT PROTEIN SCAFFOLDS FOR THE DESIGN OF FUNCTIONAL NANOSTRUC- The advent of Next Generation Sequencing methodologies has revolutionized TURES AND BIOMATERIALS our ability to discover novel peptide and protein binders using directed evolution Aitziber Lopez Cortajarena (1), Antonio Aires, Sara H. Mejias, Javier López An- methodologies such as phage, yeast, and mRNA Display. Traditional methodol- darias, Giovanna Ghirlanda, Teresa Gonzalez, Nazario Martín, Carmen Atienza ogies utilizing Sanger Sequencing have often discovered weak affi nity binders to (1) CIC biomaGUNE targets of interest that could not be progressed further without added experimen- tation or the use of expensive resources to further develop. We will describe the Proteins are the most versatile biological building blocks, composed of amino application of Next Generation Sequencing within our current hit-to-lead protein acids offering rich chemistry. Proteins present enormous diversity in 3D structures engineering pipeline as well as give an overview of several cheminformatics and that translates into amazing functional diversity. Thus, proteins have great po- bioinformatics applications we are developing to help us fully characterize our tential for use as building blocks in order to construct tailored designed systems, libraries and selections to identify potential therapeutic lead matter. including nanofabrication and generation of novel protein-based biomaterials. We explore the potential of proteins as building blocks toward the generation of functional nanostructures and bioinspired materials for applications in nanobio- technology and nanomedicine. In particular, our main objective is to develop versatile platforms based on simple protein building blocks for the fabrication of 68 69 #PS32 USING DEEP MUTATIONAL SCANNING TO PROBE PROTEIN FUNCTION, STRUC- TURE AND REGULATION Abstracts Doug Fowler (1) TPS Award Winners & Speakers (1) University of Washington Mutagenesis is a fundamental tool for understanding the relationship between STRUCTURAL AND MECHANISTIC STUDIES ON THE DYNAMIN GTPASE protein sequence, structure and function. Deep mutational scanning, which Olivier Daumke (1) can reveal the consequences of tens of thousands of mutations simultaneously, (1) Max-Delbrueck-Center for Molecular Medicine is empowering mutational analysis. I will discuss applications of deep mutational scanning to reveal new mechanisms of kinase regulation, gain insight into the Dynamin is a mechano-chemical GTPase that oligomerizes at the neck of clath- determinants of protein abundance inside cells and better understand protein rin-coated vesicles and catalyzes vesicle scission in a GTP hydrolysis dependent structure. I will also describe improvements in the scale, accuracy and range of fashion. Here, I present our structural analyses on various dynamin superfamily applications of mutational scanning approaches. members, which clarifi es the assembly and membrane regulation. Using a com- bination of biochemical and computational approaches, we obtain a mecha- ALLOSTERIC TUNING OF HSP70 MOLECULAR CHAPERONES nistic model for the action of dynamin at the vesicle neck. Lila Gierasch (1), Wenli Meng, Natalie McArthur, Eugenia Clerico, Alexan-

dra Pozhidaeva, Charles English DISEASE MUTATIONS AND POST-TRANSLATIONAL MODIFICATIONS ALTER (1) Department of Biochemistry & Molecular Biology, University of Massa- DISORDERED PROTEIN LIQUID-LIQUID PHASE SEPARATION chusetts Amherst Nicolas Fawzi (1) (1) Brown University The 70-kDa heat shock proteins, Hsp70s, are molecular chaperones that per- form a wide range of critical cellular functions. They assist in the folding of newly The mechanistic basis for disordered domain functional liquid-liquid phase synthesized proteins, facilitate assembly of specifi c protein complexes, shepherd separation (LLPS) and protein inclusion formation in neurodegenerative disease proteins across membranes, and prevent protein misfolding and aggregation. remains poorly understood. This gap persists due to a lack of direct, atomical- Hsp70s perform these functions by a conserved mechanism that relies on allosteric ly-detailed structural information. Here, I present results using NMR spectroscopy cycles of nucleotide-modulated binding and release of client proteins, with the and simulation to visualize structure and interactions of several human RNA-bind- participation of co-chaperones, including J-proteins and nucleotide exchange ing proteins with aggregation-prone low complexity (LC) domains that undergo factors. Current models for Hsp70 allostery have come from extensive study of the LLPS and aggregate in ALS and frontotemporal dementia. First, we focus on bacterial Hsp70, DnaK. While providing a likely common mechanistic framework, sequence factors regulating LLPS. In the Fused in Sarcoma (FUS) LC domain, we extending our understanding to eukaryotic Hsp70s is extremely important because fi nd that phosphorylation disrupts LLPS. In hnRNPA2, asymmetric dimethylation of their central roles in cellular physiology. In this study, we examined the allosteric of arginine residues disrupts arginine-aromatic residue contacts and decreases behavior of the eukaryotic inducible cytoplasmic Hsp70, HspA1, which has 46% LLPS. Because many phase-separating RNA-binding proteins contain phos- sequence homology with DnaK, and found signifi cant differences from that of phorylation and methylation sites, understanding the biophysical chemistry of DnaK. We fi nd that HspA1 favors a state in which the nucleotide-binding domain modifi cations will be important. Second, we examine factors distinguishing LLPS (NBD) and substrate-binding domain (SBD) are intimately docked signifi cantly and aggregation. The hnRNPA2 P298L disease variant removes a conserved, more than DnaK does. Past work established that the NBD-SBD interface and the ß-sheet breaking proline to enhance aggregation, suggesting an important helical lid-ßSBD interface govern the allosteric landscape of DnaK, and here we role for prolines in aggregation-prone LC domains. Third, we examine the role of identifi ed sites on these interfaces that differ between HspA1 and DnaK. These structured domains in modulating LC domain LLPS. In contrast to disorder of FUS results underline the tunability of Hsp70 functions by modulation of allosteric inter- and hnRNPA2 LC domains after LLPS, LLPS of TDP-43 is mediated in part by par- faces through evolutionary diversifi cation and also suggest sites where the binding tially-structured a-helical assembly that is disrupted by ALS-associated mutations. of small molecule modulators could infl uence Hsp70 function. Furthermore, LLPS of full-length TDP-43 is enhanced by weak linear polymerization of the globular N-terminal domain. Substitution at a conserved phospho-site de- creases LLPS in vitro and in cells and disrupts splicing activity. Our work points to the potential for post-translational modifi cation to alter assembly, function, and pathological interactions of disease-associated disordered domains. 70 71 #PS32 EXPANDING ROLES FOR THE ESCRT MACHINERY Phyllis Hanson (1) Abstracts (1) Washington University School of Medicine TPS Award Winners & Speakers The ESCRT-III machinery comprises a collection of proteins that form polymeric RNA STRUCTURE ENCODES SPECIFICITY IN A POLYQ PROTEIN PHASE SEPARATION fi laments involved in membrane remodeling and fi ssion in numerous contexts, notably during the formation of multivesicular endosomes. Recent studies high- Amy Gladfelter (1) Erin M. Langdon, Peggy Billingsly, Amirhossein Ghan- light additional roles for ESCRT proteins in an increasing range of membrane bari Niaki, Grace McLaughlin, Chase Weidmann, Therese Gerbich, Christi- remodeling reactions that may not be limited to the topology traditionally na M. Termini, Kevin M. Weeks, Sua Myong associated with ESCRT pathway function. I will discuss new insights into ESCRT-III (1) Department of Biology, University of North Carolina at Chapel Hill function on endolysosomal membranes, with a particular focus on their involve- ment in repair of transiently damaged endolysosomes. A variety of cell structures assemble via liquid-liquid phase separation (LLPS) to form compartments without membranes in both the cytoplasm and nucleus. RNA CHAPERONING SNARE ASSEMBLY TO CONTROL MEMBRANE FUSION is a central driver of LLPS, however it is not well understood how RNA-based liquid Fred Hughson (1) droplets establish and maintain individual identities. We have found that a polyQ- (1) Princeton University rich RNA-binding protein (Whi3) undergoes LLPS in the presence of specifi c mRNAs in order to pattern cell growth and division. Using this system, we have investigat- ed how mRNAs are recruited to or excluded from liquid compartments based The compartmentalization of eukaryotic cells demands an intracellular transpor- on their sequence and ability to self-associate. We have found that the specifi c tation system. Cargo is transported within vesicles that bud from one compart- secondary structure of mRNAs determines which RNAs co-assemble into the same ment, travel through the cell, and deliver their contents by fusing with another droplets and which are segregated to distinct structures. Additionally, polyQ-pro- compartment (or, in the case of exocytosis, with the plasma membrane). tein binding elicits distinct conformations in different target RNAs imparting a sec- Underlying this intricate choreography is a set of proteins and protein complexes ond layer of specifi city. The implications of sequence-encoded shape information responsible for the creation, movement, docking, and fusion of vesicles. Our lab in RNA will be discussed in the context of how molecular scale interactions lead seeks to understand the design principles that endow these protein nanoma- to mesoscale physical properties of phase separated compartments. How the chines with the ability to manipulate membrane vesicles, thereby powering a diverse array of RNA-rich liquid compartments coexist in a single cell remains a bustling intracellular transportation network. In this talk, I will focus on our recent X-ray crystallographic, biochemical, and single-molecule biophysical studies fundamental challenge in understanding the cell biology of phase separation. suggesting that Sec1/Munc18 (SM) family proteins play a key role in chaperoning the assembly of fusion-competent SNARE complexes. The generality and poten- PROTEIN MATERIALS: FROM NATURE TO NANOTECHNOLOGY tial implications of these fi ndings will be discussed. Tijana Grove (1) (1) Virginia Tech EVOLUTION OF AN ENZYME FROM A SOLUTE-BINDING PROTEIN Colin Jackson (1) Proteins and protein assemblies are the biological workhorses that carry out vital (1) Australian National University functions in all living organisms. The Grove lab is interested in translating fundamental knowledge and principles of how proteins operate in nature to the growing fi eld of nanotechnology for the design of multifunctional, dynamic materials. Herein, I will Much of the functional diversity observed in modern enzyme superfamilies orig- present our most recent work on the repeat-protein biomaterials that self-assemble inates from molecular tinkering with existing enzymes. New enzymes frequently through the combination of head-to-tail stacking and weak dipole-dipole interac- evolve from enzymes with latent, promiscuous activities, and often inherit key tions. These ion and proton conducting materials exhibit anisotropic properties at features of the ancestral enzyme, retaining conserved catalytic groups and stabi- biologically relevant length-scales, nano to micro, and relevant time scales, millisec- lizing analogous intermediates or transition states. While experimental evolutionary onds to seconds. I will further highlight the tunable anisotropic nano and meso-scale biochemistry has yielded considerable insight into the evolution of new enzymes morphologies, which direct the material' bending, twisting, or curling in response to from existing enzymes the emergence of catalytic activity de novo remains changes in relative humidity and electric potential. poorly understood. Although certain enzymes are thought to have evolved from non-catalytic proteins, the mechanisms underlying these complete evolutionary transitions have not been described. Here we show how the enzyme cyclohexadi- enyl dehydratase (CDT) evolved from a cationic amino acid-binding protein be- longing to the solute-binding protein (SBP) superfamily. Analysis of the evolutionary 72 73 REPURPOSING RIBOSOMES FOR SYNTHETIC BIOLOGY #PS32 Michael Jewett (1) Abstracts (1) Northwestern University TPS Award Winners & Speakers The Escherichia coli ribosome is a 2.4 MDa molecular machine made up of 57 RNA and protein parts. To support bacterial log phase growth with a 40-minute trajectory between reconstructed ancestors and extant proteins showed that the doubling time, ribosomes must be produced at a rate of ~8 ribosomes per second. emergence and optimization of catalytic activity involved several processes. The Once assembled, these ribosomes can synthesize sequence-defi ned polymers emergence of CDT activity was potentiated by the incorporation of a desolvated of amino acids with elongation rates of up to 20 amino acids per second and an general acid into the ancestral binding site, which provided an intrinsically reac- accuracy of ~99.99%. The rapid rate of synthesis and incredible catalytic capabil- tive catalytic motif, and reshaping of the ancestral binding site, which facilitated ity motivate efforts to understand the systems biology of ribosome biogenesis and enzyme-substrate complementarity. Catalytic activity was subsequently gained function, as well as to create engineered variants with altered function. As a result, via the introduction of hydrogen-bonding networks that positioned the catalytic the construction of engineered ribosomes has emerged as a defi ning challenge in residue precisely and contributed to transition state stabilization. Finally, catalytic synthetic biology, with opportunities to build minimal cells, enable dual translation activity was enhanced by remote substitutions that refi ned the active site structure systems in cells, and catalyze a new paradigm for the synthesis and evolution of and reduced sampling of non-catalytic states. Our work shows that the evolu- abiological polymers. Unfortunately, the requirement of cell viability severely limits tionary processes that underlie the emergence of enzymes by natural selection in the mutations that can be made to the ribosome. In this presentation, I will discuss the wild are mirrored by recent examples of computational design and directed my group's efforts to address this critical limitation both in vivo and in vitro. In vivo, evolution of enzymes in the laboratory. we report the fi rst fully orthogonal ribosome-mRNA system by creating ribosomes with tethered subunits (termed Ribo-T). In vitro, we established a cell-free ribosome A MOLECULAR MOVIE OF STRUCTURAL CHANGES IN THE LIGHT-DRIVEN PROT construction platform, termed iSAT (integrated synthesis, assembly, and translation of ribosomes) to build modifi ed ribosomes in test tubes. Our results set the stage REMEMBERING THE PAST: A NEW FORM OF PROTEIN-BASED INHERITANCE to transform synthetic biology by repurposing the translational apparatus to syn- Daniel Jarosz (1) thesize novel sequence-controlled polymers and functional biomaterials with an (1) Stanford University expanded chemistry of life.

During their lifetimes, individuals commonly experience transient changes in COMPLEX PHENOTYPIC LANDSCAPE OF A SIMPLE PHASE-SEPARATED gene expression as a result of different environmental stimuli. These responses are PROTEIN SYSTEM classically thought to have no heritable infl uence once they decay. However, we Emmanuel Levy (1), Meta Heidenreich, Joseph Georgeson, Emanuele have recently discovered that such stimuli frequently induce self-perpetuating changes in protein conformations. This occurs most commonly in proteins that Locatelli, Yotam Nadav, Saroj Nandi, Lorenzo Rovigatti, Avital Steinberg, regulate information fl ow: chromatin modifying enzymes, transcription factors, and Jonathan Doye, Samuel Safran RNA binding proteins. These self-templating changes in protein conformation can (1) Department of Structural Biology, Weizmann Institute of Science, be broadly defi ned as prions, although their structures do not usually match the cross-beta sheet amyloids of the archetypical prion PrP. However, like known pri- Phase separated protein assemblies span a vast phenotypic landscape of ons, corresponding changes in protein function are heritable from one generation size, shape, and material state. The rapidly growing catalog of mesoscale to the next without any change to the genome. In this sense, such protein-based assemblies calls for understanding how their macroscopic phenotypes relate to inheritance represents an extreme form of epigenetics. We have begun to char- atomic properties of their constituent molecules. To cast light on this relation- acterize the biochemistry of these epigenetic elements and investigate their infl u- ship, we employed synthetic biology and designed pairs of protein building ence on disease, development, and evolution. Our results provide a mechanistic blocks endowed with controllable valence and affi nity of intermolecular understanding of a form of inheritance that is quasi-Lamarckian in character, but interaction. We analyzed multiple pairs expressed across thousands of cells, fi rmly rooted in a Darwinian framework of mutation and natural selection. Lessons revealing that phase-diagrams measured in vivo are expected from polymer learned provide insight into mechanisms of pathological and benefi cial protein theory. Further, the material state of these phase-separated assemblies could aggregation alike, and how they might be modulated therapeutically. be tuned from gel to liquid by point mutations decreasing the cross-interaction affi nity. Remarkably, despite its synthetic and straightforward nature, this system showed complex emergent properties that include cell-growth-dependent phase-separation and asymmetric partitioning upon cell division. This system provides a well-controlled molecular toolkit to model mesoscale assembly from fi rst principles, and for designing advanced biomaterials and scaffolds. 74 75 #PS32 SUBSTRATE PROCESSING, CONFORMATIONAL CHANGES, AND MECHANO- CHEMICAL COUPLING OF THE 26S PROTEASOME - A FINE-TUNED MOLECU- Abstracts LAR MACHINE TPS Award Winners & Speakers Andreas Martin (1), Jared A.M. Bard, Eric R. Greene, Ellen A. Goodall, Ken C. Dong, and Andreas Martin ELECTROPHILE FRAGMENT SCREENING AS A RAPID METHOD FOR COVALENT (1) Department of Molecular & Cell Biology and Howard Hughes Medical PROBE DISCOVERY Institute, UC Berkeley Nir London (1) (1) The Weizmann Institute of Science Ubiquitin-dependent substrate degradation by the 26S proteasome is a tightly regulated multi-step process that includes ubiquitin-chain binding, engagement, Fragment based screening has seen tremendous growth over the past few years unfolding, and translocation of the substrate polypeptide, translocation-cou- and is currently a widely accepted method for early small molecule hit discov- pled de-ubiquitination, and substrate hydrolysis. During this degradation cycle, ery. Still, a major limiting factor in screening fragments, is the typical low affi nity of the proteasome goes through major conformational changes that appear to the hits, which necessitates very sensitive assays. Fragments that are able to form facilitate the various steps of substrate processing. To directly study the kinetics a covalent bond with their target protein can overcome this challenge. Howev- and coordination of individual processing steps, we have developed a series of er, such electrophilic fragments were considered to be non-selective and little to fl uorescence and FRET-based assays that rely on the incorporation and labeling no screening was performed in this space. We have culled a library of 993 mild of unnatural amino acids in recombinant proteasomes. The site-specifi c place- electrophilic fragments. We have characterized them by a new high-throughput ment of fl uorescent dyes allows for the fi rst time to follow a protein substrate method for evaluation of thiol reactivity and importantly by screening a diverse through degradation, dissect individual steps, and study the coupled conforma- panel of ten cysteine containing proteins. We fi nd that highly reactive fragments tional changes in the proteasome. By using substrates with various architectures, are scarce on the one hand and can be easily weeded on the other. We were we gain a better understanding of how a substrate’s geometry and ubiquitin able to fi nd quality hits for most of the screened proteins. We demonstrate for modifi cations affect the degradation rate, which processing steps are rate-limit- two test systems, the deubiquitinase OTUB2 and the pyrophosphatase NUDT7, ing, and how the proteasome may prioritize its substrates in the cell. Furthermore, how combination with high-throughput crystallography lead rapid progression to we have identifi ed an allosteric network between proteasome subcomplexes potent and selective probes - the fi rst reported for either of these enzymes. This that controls the major conformational transitions of the holoenzyme. Disrupting study highlights the potential of electrophile fragment screening as a practical this network inhibits substrate degradation at particular stages, highlighting how and effi cient tool for covalent ligand discovery as long as the electrophile selec- the proteasome molecule machine depends on adopting distinct states in a tivity is accounted for. controlled manner to coordinate the individual substrate-processing steps.

POSTEVOLUTIONARY GENETIC VARIATION, 3D STRUCTURE AND DESIGN HOW THE PROTEASOME SELECTS ITS TARGETS FOR DESTRUCTION Debora Marks (1), Systems Biology Andreas Matouschek (1), Amit Gautam, Takuya Tomita, Kazu Takahashi, (1) Harvard Medical School Kimberly Bowen, Caroline Davis, Frank Medina, Chris Yellman, Dennis Wylie, Kirby Martinez-Fonts, Suzanne Elsasser, Dan Finley What can we do with a million or a billion genomes? Understanding how vari- (1) The University of Texas at Austin ation across genomes shapes the properties of biomolecules, cells, and organ- isms is a foundational question in biomedicine and biotechnology. I will present The proteasome can degrade effectively any protein but does so with exqui- examples of how generative modeling of evolutionary or synthetic genetic site specifi city. Proteins are targeted to the proteasome through a two-part variation can give surprisingly direct answers to questions about 3D structures, degradation signal or degron. The degron consists of a proteasome-binding dynamics and the effects of mutations. Evolutionary couplings have now been tag, typically a polyubiquitin chain, and a proteasome initiation site in the form used to determine thousands of otherwise unknown protein structures, increas- of an unstructured region within the substrate. We investigate how the prote- ingly used to determine alternative structural states and accelerate experimen- asome recognizes both components of the degron and how the two compo- tal approaches to large dynamic complexes. Our new work extends from the nents contribute to substrate selection. undirected models of genetic variation to deep directed models for genetic variation. From purely unsupervised learning, we double the improvement of prior-art for predicting the effects of mutations. I will introduce challenges for extending these methods to diverse biomedical and engineering applications. 76 77 between Asp85 and Thr89 was lost, which in turn interrupted connectivity to the #PS32 extracellular side of the protein. The resulting cascade of structural changes Abstracts throughout the protein provided unprecedented insights into how structural TPS Award Winners & Speakers changes in bR conspire to achieve unidirectional proton transport. EXTENSIBLE PROTEIN SCAFFOLDS BASED ON BETA SOLENOIDS A SHAPE-SHIFTING PROTEIN COORDINATES TIMEKEEPING BY THE CYANO- James Murray (1), James T. MacDonald BACTERIAL CIRCADIAN CLOCK (1) Imperial College Carrie L. Partch (1,2), Jeffrey Swan, Joel Heisler, Courtney Dailley, Susan S. Golden), Andy LiWang Protein design is in general hard, as beyond small domains the all-atom folding (1) Department of Chemistry & Biochemistry, University of California Santa problem is intractable. To solve this, we propose an approach based on extensi- Cruz, (2) Center for Circadian Biology, University of California San Diego ble repetitive scaffolds. The scaffold can be incrementally elaborated, allow- ing complexity to be built up in stages, without requiring large-scale all-atom Circadian rhythms are an ancient evolutionary adaptation found across the design. The rigid scaffolds can also be used to design crystal lattices or closed domains of life, synchronizing behavior and physiology to the daily solar cycle for point group assemblies. We have developed a series of scaffold proteins, Beta1, optimal fi tness. In cyanobacteria, timekeeping is established by three Kai proteins based on the RFR (repeat fi ve residues) family of beta solenoid scaffolds. The (KaiA, B and C) that form distinct protein complexes throughout the day, compris- initial scaffold protein was produced by drawing residues from an RFR frequen- ing a molecular clock that keeps ~24-hour timing. Remarkably, this protein-based cy table, so the middle 120 residues have no evolutionary "memory". We have clock exhibits accurate, temperature-compensated timekeeping in the presence solved the structures of length variants, and also produced scaffolds with loop of only ATP in vitro. The LiWang lab recently discovered that KaiB undergoes a elaborations from the central core. The loop structures have been designed rare transition from its tetrameric ground state to a rare fold-switched, monomeric using a novel de novo all-atom approach, rather than being assembled from signaling state that is needed to bind KaiC and advance the clock in its evening fragments of known structure. The loops are folded in accordance with the origi- phase. To address the structural basis for this nighttime complex, we locked KaiB nal design. The potential of this approach to design will be discussed. into its fold-switched state, allowing us to solve crystal and NMR structures of four key complexes that demonstrate how KaiB docks cooperatively on the KaiC ON PUMP BACTERIORHODOPSIN hexamer to recruit KaiA and the input/output protein CikA. A new structure of Eriko Nango (1), So Iwata the output protein SasA bound to KaiC illustrates how KaiB uses structural mimicry (1) RIKEN SPring-8 Center, Graduate School of Medicine, Kyoto University to compete with SasA binding at dusk. Collectively, these structures reveal how protein interactions regulate day/night transitions and highlight the essential role of Bacteriorhodopsin (bR) is a light-driven proton pump containing an all-trans ret- fold-switching by KaiB for control of timekeeping, input, and output signaling in the inal and harvests the energy content of light to drive conformational changes cyanobacterial circadian clock. leading to unidirectional proton transport. The all-trans retinal undergoes isom- erization to the 13-cis confi guration by light absorption, initiating a photo-cycle REPETITIVE PROTEINS ON THE SURFACE OF GRAM-POSITIVE BACTERIA and creating a sequence of spectral and structural changes. Jennifer Potts (1), Lotte Van Beek, James Gilburt, Fiona Whelan, Alex G. Bateman, Christoph G. Baumann We used time-resolved (TR) serial femtosecond crystallography (SFX) at the (1) University of York SPring-8 Angstrom Compact Free Electron Laser (SACLA) for recording a three-dimensional movie of structural changes in bR at room-temperature. The Cell wall-attached proteins from Gram-positive bacteria play important roles in recent advent of intense, femtosecond X-ray pulses from X-ray free-electron infection. This includes attachment to host tissues and prosthetic surfaces, and laser (XFEL) has enabled the acquisition of diffraction patterns from protein inter-bacterial interactions during biofi lm formation on medical devices. Several of microcrystals before the onset of radiation damage. TR-SFX data were collected these proteins have a common organization that includes a globular N-terminal from light-adapted bR microcrystals following photo-activation with a nanosec- domain, a repetitive central region and a cell-wall attachment site near the C-ter- ond laser pulse for ?t = 16 ns~1725 μs. Our data revealed that an initially twisted minus. We use a variety of biophysical and structural techniques including NMR retinal displaced Trp182 and Leu93 toward the cytoplasm and allowed a water spectroscopy, X-ray crystallography, small angle X-ray scattering and single-mole- molecule (Wat452) to order between Leu93, Thr89 and the Schiff base (SB) on cule high-resolution fl uorescence imaging to understand the relationship between the retinal in the L-state. Hydrogen-bonding interactions from the protonated SB structure and function. Our work has revealed that the repetitive regions can form to Wat452 and Thr89, created a pathway for proton transfer to a proton accep- a rod-like structure from a single protein chain that presumably acts to project the tor, Asp85. Once a proton was transferred, the hydrogen-bonding interaction functional N-terminal domain from the bacterial cell surface. We will also discuss 78 79 of molecular recognition in intrinsically disordered proteins in atomistic detail. In #PS32 unbiased MD simulations of an intrinsically disordered protein and its physiolog- Abstracts ical binding partner, for example, we observe a large number of spontaneous folding-upon-binding events, allowing us to carefully dissect and characterize the TPS Award Winners & Speakers observed binding mechanisms. In a second application, unbiased MD simulations the properties of the individual domains and their ability to exist in highly repetitive of the intrinsically disordered protein a-synuclein with a small molecule ligand sequence arrays despite evidence in other multi-domain proteins of evolutionary reproduce a binding interaction observed by NMR spectroscopy experiments. pressure against tandem arrangement of highly identical domains. These simulations have enabled us to rationalize the molecule’s affi nity for the experimentally observed binding site using a dynamic binding mechanism model AMYLOIDS: FROM THE ORIGIN TO THE END OF LIFE in which a-synuclein remains fl exible as it interacts with the small molecule in a va- Roland Riek (1), Beat Meier, Juan Gerez, Marielle Wälti, Jason Greenwald, riety of binding modes. We are currently exploring the possibility of using dynamic Saroj Rout, Carolin Seuring binding mechanisms observed in MD simulations to rationally design molecules (1) ETH Zurich that exhibit improved binding to intrinsically disordered proteins.

Protein aggregation into amyloids is both associated with neurodegenerative CIRCADIAN RHYTHMS FROM COUPLED ATPASE DOMAINS diseases as well as function such as hormone storage in the pituitary. The structure Michael Rust (1, 2), Lu Hong, Connie Phong, Eugene Leypunskiy, Aaron Dinner determinations of amyloid fi brils by solid state NMR at atomic resolution establishes (1) Graduate Program in Biophysics, University of Chicago, (2) Department both a structure-function as well as a structure-disease relationship as demon- of Molecular Genetics and Cell Biology, University of Chicago, strated with the 3D NMR structures of the HET-s prion, Abeta(1-42) fi brils associated with Alzheimer’s disease, and of the hormone beta-endorphin stored in secretory Three proteins from photosynthetic cyanobacteria, KaiA, KaiB, and KaiC, form a granules in an amyloid state. remarkable oscillating reaction in vitro that produces coherent 24-hour oscilla- tions in the phosphorylation state of KaiC. Because this minimal biochemical sys- NMR can also be used in cells. The in-cell NMR of a-synuclein associated with tem has many of the features of circadian rhythms in living organisms, it presents Parkinson’s disease shows that a-synuclein transiently interacts with chaperones in the opportunity to understand the biophysical basis of rhythmic physiology. The cells. Chaperone down regulation induces a-synuclein membrane binding and past decade as seen an explosion in biochemical and biophysical understand- aggregation. ing of this oscillator, but many fundamental questions remain. I will review pre- vious work on this system, including our efforts to study entrainment to light-dark Based on the structure-activity relationships of amyloid, we and others developed cycles using the purifi ed protein system. Finally, I will discuss our recent use of mo- to so called amyloid world hypothesis, which states that peptide amyloids may lecular dynamics simulations to understand the mechanism of oscillating activity have played an important role in the origin of life. Experimental support in the area in KaiC, the core enzyme in the clock that consists of hexameric ring of tandem of enzymatic active peptide amyloids, amyloid generation under prebiotic condi- ATPase domains which can undergo autophosphorylation. This analysis points to tion and template-assisted peptide synthesis in the amyloid are presented. a key role for the regulation of product release in controlling the catalytic cycle.

IMPROVED PHYSICAL MODELS ENABLE THE INVESTIGATION OF MOLECULAR REC- THE RAPID WAY TO DISCOVER BIOACTIVE PSEUDO-NATURAL PEPTIDES WITH OGNITION IN INTRINSICALLY DISORDERED PROTEINS AT ATOMISTIC RESOLUTION MACROCYCLIC SCAFFOLD Paul Robustelli (1) Hiroaki Suga (1) (1) D.E. Shaw Research (1) The University of Tokyo

Molecular dynamics (MD) simulation can serve as a valuable complementary The genetic code is the law of translation, where genetic information encoded tool to experiments in characterizing the structural and dynamic properties of in RNA is translated to amino acid sequence. The code consists of tri-nucleotides, intrinsically disordered proteins. The utility of MD simulation depends, however, on so-called codons, assigning to particular amino acids. In cells or in ordinary cell- the accuracy of the underlying physical models (or “force fi elds”). By comparing free translation systems originating from prokaryotes, the usage of amino acids is long-timescale simulations of ordered and disordered proteins to experimental generally restricted to 20 proteinogenic (standard) kinds, and thus the expressed data, we have systematically identifi ed limitations in current physical models and peptides are composed of only such building blocks. To overcome this limitation, have developed new force fi elds that provide substantially improved accuracy we recently devised a new means to reprogram the genetic code, which allows in simulations of disordered proteins while maintaining state-of-the-art accuracy us to express non-standard peptides containing multiple non-proteinogenic amino for folded proteins. These new force fi elds have enabled us to study mechanisms acids in vitro. This lecture will describe the development in the genetic code 80 81 #PS32 METALLO-ß-LACTAMASES: A TUG OF WAR BETWEEN BACTERIA AND THE INMUNE SYSTEM FOR THE AVAILABLE ZN(II) Abstracts Alejandro Vila (1), Guillermo Bahr, Estefania Giannini, Antonela R. Pala- TPS Award Winners & Speakers cios, Ma. Agustina Rossi, Juliana Delmonti, Carolina López, Pablo E. Toma- tis, Lisandro J. González reprogramming technology that enables us to express natural product-inspired (1) Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET) – non-standard peptides and pseudo-natural products. The technology involves (1) Universidad Nacional de Rosario effi cient macrocyclization of peptides, (2) incorporation of non-standard amino acids, such as N-methyl amino acids, and (3) reliable synthesis of libraries with the Metallo-ß-lactamases (MBLs) are Zn(II)-dependent ß-lactamases that constitute complexity of more than a trillion members. When the technology is coupled with the latest resistance mechanism of pathogenic and opportunistic bacteria against an in vitro display system, referred to as RaPID (Random non-standard Peptide carbapenems, considered as last resort drugs. Zn(II) binding is critical in the bacterial Integrated Discovery) system as a novel “molecular technology”, the libraries of periplasm, not only to activate these enzymes and provide resistance, but also to natural product-inspired macrocycles with a variety ring sizes and building blocks stabilize the protein scaffold. During infection, the immune system elicits a response can be screened (selected) against various drug targets inexpensively, less labo- that scavenges the available Zn(II), impacting in the activity of stability of these riously, and very rapidly. This lecture will discuss the most recent development of proteins, thus compromising bacterial survival. However, the activity and stability of their technology and therapeutic applications toward drug discovery innovation. these proteins in vitro does not necessarily correlate with those in the periplasm. Thus, the whole picture must be described by means of an integrated approach. THE FORMATION OF FUNCTIONAL AMYLOID FIBRILS BY VIRAL PROTEINS THAT MODULATE HOST CELL DEATH PATHWAYS We developed a strategy aimed to correlate the biochemical and biophysical Margaret Sunde (1), Chi L. L. Pham, Merryn Strange, Niruk Shanmugam, features in purifi ed enzymes with those in the bacterial periplasm, ultimately lead- Max. O. D. G. Baker, Megan Steain, Emma Sierecki, Yann Gambin ing to the selected phenotype, i.e., resistance to antibiotics. This strategy allows (1) School of Medical Sciences and Sydney Nano, University of Sydney, us to dissect the molecular features that are tailored by accumulating mutations NSW 2006, Australia during evolution to endure the action of the immune system response. We have applied this approach to in vitro evolved protein in the laboratory, as well as to Herpes viruses express proteins that are primarily implicated in inhibiting the host natural allelic variants selected in clinical strains. This has allowed us to account for programmed cell death pathways apoptosis and necroptosis. We show that two the epistatic interactions between mutations at a structural level. protein inhibitors of necroptosis, the protein M45 from murine cytomegalovirus and the ICP6 protein expressed by Herpes simplex virus-1, are able to form amyloid We have also studied the natural evolutionary landscape of allelic variants of a fi brils with hallmark physical characteristics. We demonstrate that the RIP homo- clinically relevant lactamase (NDM), that has been shaped by Zn(II) deprivation typic interaction motif (RHIM) within these proteins renders them amyloidogenic. conditions. Thus, natural NDM variants with enhanced Zn(II) binding affi nity have Additionally, we have characterized a previously unrecognised RHIM in the ORF20 been selected, overriding the most common evolutionary pressure acting on protein from Varicella zoster virus. The receptor interacting kinases RIPK1 and RIPK3 catalytic effi ciency. and the viral sensor ZBP1 contain RHIMs that support the formation of complex- es that signal for necroptosis, downstream of death receptor activation or viral THE UPS AND DOWNS OF PROTEIN EXPRESSION REGULATION infection. Li et al were the fi rst to demonstrate that the RHIM-based RIPK1: RIPK3 Christine Vogel (1) complex is a functional hetero-amyloid structure (2012, Cell, 150:339-350). (1) NYU

We have used a wide range of biophysical techniques, including single molecule Gene expression is regulated by four major processes: transcription, translation, fl uorescence studies, to demonstrate that viral RHIM-containing proteins are able and RNA and protein degradation. These processes are adjusted, in different to form hetero-oligomeric amyloid fi brils through co-assembly with cellular RIPK1, ways, when the cells respond to a stimulus. Many pathways are known, but their RIPK3 and ZBP1. We fi nd that the incorporation of a viral protein into RIPK1:RIPK3 precise interaction over time is not well understood. In our lab, we use multiple amyloid fi brils alters the structure and stability of the amyloid complexes. Our results time series datasets — on protein and mRNA expression changes and chang- demonstrate that the ability of these viral proteins to form competing or “decoy” es in the binding of ribosomes and other proteins — in combination with mass amyloid fi brils with cellular RHIM-containing proteins likely contributes to the sup- action models and other approaches to disentangle the contributions of the dif- pression of programmed cell death by this family of viruses. ferent levels of regulation and generate hypotheses on regulatory mechanisms. We focus on yeast and mammalian cells responding to stress of the endoplasmic reticulum but have expanded these studies in a variety of directions. 82 83 photoswitchable fl uorescent protein captured by time-resolved serial femtosec- #PS32 ond crystallography. Nature Chemistry 10: 31-37 Abstracts EVOLUTIONARY OUTCOMES OF CRISPR-ANTI-CRISPR CONFLICT TPS Award Winners & Speakers Blake Wiedenheft (1) CRISPR-CAS MEDIATED CLEAVAGE OF INVADING NUCLEIC ACIDS (1) Montana State University Yanli Wang (1), Jiuyu Wang, Liang Liu, Jiazhi Li, Xueyan Li, Hongtu Zhao (1) Institute of Biophysics, Chinese Academy of Sciences Viruses that infect bacteria (i.e., bacteriophages) are the most abundant biologi- cal entities on earth and the selective pressures imposed by these pervasive pred- Bacteria and archaea are protected against invading nucleic acids from phages ators have a profound impact on the composition and the behavior of microbial and plasmids because of CRISPR (Clustered Regularly Interspaced Short Palin- communities in every ecological setting. Our work aims to understand the mecha- dromic Repeats)-Cas (CRISPR associated proteins) systems, which are RNA-guided nisms that bacteria use to defend themselves from viral infection and the counter prokaryotic adaptive immune system. CRISPR-Cas systemsare found in nearly measures that viruses use to subvert bacterial immune systems. Confl ict between half of all bacteria studied so far, as well as in the majority of archaea. However, viruses and their hosts immune systems, promotes biological innovation. Our work throughout evolution, this host defense system has not resulted in the eradication aims to determine molecular structures of cellular machines that are responsible of phages, suggesting that phages have evolved counter strategies to thrive for waging these biological battles. within bacteria despite these mechanisms. Thus, both bacterial CRISPR system and phage anti-CRISPR system are part of a continuing evolutionary battle between bacterial host and their bacteriophage invaders. We provided signifi cant insights into the molecular mechanism for how CRISPR-Cas systems defend against the invading nucleic acids from phages and how phages counteract the CRISPR-Cas systems by anti-CRISPR proteins.

ULTRA-FAST PHOTOSWITCHING IN FLUORESCENT PROTEINS OBSERVED BY TIME-RESOLVED SERIAL FEMTOSECOND CRYSTALLOGRAPHY Martin Weik (1) (1) Institut de Biologie Structurale

Super-resolution optical microscopy has revolutionized in vivo imaging by the mark-up of biological cells to be imaged using photoswitchable fl uorescent pro- teins. These molecular switches can be reversibly toggled from a fl uorescent (on) to a non-fl uorescent (off) state further to excitation by a light fl ash. For the purpos- es of rational design, it is necessary to understand the mechanism of photo-switch- ing, which involves ultra-rapid transient states. Our consortium (see author list of [1]) has employed time-resolved serial femtosecond crystallography at an X-ray free electron laser to identify the transient structure of the photoswitchable fl uorescent protein rsEGFP2 in its excited state, and to observe its chromophore in a twisted state, midway between the stable confi gurations of the on and off states. This observation has been confi rmed by simulations and has allowed us to rationally design a mutant with a two-fold increased photoswitching quantum yield.

[1] Coquelle N, Sliwa M, Woodhouse J, Schirò G, Adam V, Aquila A, Barends TRM, Boutet S, Byrdin M, Carbajo S, De la Mora E, Doak RB, Feliks M, Fieschi F, Foucar L, Guillon V, Hilpert M, Hunter MS, Jakobs S, Koglin JE, Kovacsova G, Lane TJ, Lévy B, Liang M, Nass K, Ridard J, Robinson JS, Roome CM, Ruckebusch C, Seaberg M, Thepaut M, Cammarata M, Demachy I, Field M, Shoeman RL, Bourgeois D, Colle- tier J-P, Schlichting I, Weik M (2018) Chromophore twisting in the excited state of a 84 85 #PS32 POS009 Posters INTRACELLULAR CRYSTALLIZATION OF HUMAN IGGS DURING BIOSYNTHESIS: PROVIDING BIOCHEMICAL INSIGHTS INTO CRYSTAL FORMATION IN THE ER POS002 Haruki Hasegawa (1), Francis Kinderman, Randal Ketchem, Carla Forte, NORADRENALINE SUPPRESSES Α-SYNUCLEIN FIBRILLATION, BINDS WEAKLY Mei Geng, Ling Liu, Kevin Graham, Frederick Jacobsen, Ai Ching Lim TO INTERMEDIATES IN THE PATHWAY AND DISAGGREGATES THEM INTO (1) Amgen Inc. (South San Francisco, United States) Β-SHEET RICH CYTOTOXIC SPECIES Priyanka Singh (1), Rajiv Bhat POS010 (1) Jawaharlal Nehru University (New Delhi, India) THERMAL STABLE AND DETERGENT-FREE MEMBRANE RECEPTOR PROTEINS THRU GENETIC MODIFICATION POS003 Rui Qing (1), Qiuyi Han, Fei Tao, Michael Skuhersky, Shuguang Zhang STRUCTURAL ANALYSIS OF PROCASPASE-2:14-3-3 COMPLEX (1) Massachusetts Institute of Technology (Cambridge, United States) Aneta Smidova (1), Dana Kalabova, Miroslava Alblova, Tomas Obsil, Veronika Obsilova POS012 (1) Institute of Physiology of the CAS (Prague, Czech Republic) REVERSING ALLOSTERIC COMMUNICATION: FROM DETECTING THE ALLOSTERIC SITES TO INDUCING AND TUNING TARGETED ALLOSTERIC RESPONSE POS004 Wei-Ven Tee (1), Enrico Guarnera, Igor Berezovsky HUMAN PROCASPASE-2 PHOSPHORYLATION AT BOTH S139 AND S164 IS (1) Bioinformatics Institute (Singapore, Singapore) REQUIRED FOR 14-3-3 BINDING Dana Kalabova (1), Aneta Smidova, Olivia Petrvalska, Tomas Obsil, Ve- POS013 ronika Obsilova DEGRADATION OR REGULATION?: THE ROLE OF THE “SILENT” PARTNER, (1) Institute of Physiology of the CAS / 2nd Faculty of Medicine, Charles BARD1, IN BRCA1 UBIQUITIN LIGASE ACTIVITY University (Prague, Czech Republic) Mikaela Stewart (1), Elena Zelin, Tom Walsh, Jacob Corn, Mary-Claire King, Rachel Klevit POS005 (1) Texas Christian University (Fort Worth, United States); INTEGRATIVE STRUCTURE AND FUNCTIONAL ANATOMY OF A NUCLEAR PORE COMPLEX POS014 Ilona Nudelman (1), Seung Joong Kim, Javier Fernandez-Martinez, Yi Shi, DESIGN OF A FUSION PROTEIN FORMING MUTATION TOLERANT AND CHEMI- Wenzhu Zhang, Brian Chait, Michael Rout, Steven Ludtke, Christopher Akey CALLY MODIFIABLE HOLLOW NANOPARTICLE (1) Rockefeller University (New York, United States) Norifumi Kawakami (1), Erika Nasu, Kenji Miyamoto (1) Keio University (Yokohama, Japan) POS006 EXTANT FOLD-SWITCHING PROTEINS ARE WIDESPREAD POS015 Lauren Porter (1), Loren Looger APPLYING PROGRAMMABLE UBIQUITIN LIGASE TO PROBE UBIQUITIN SIGNAL- (1) HHMI, Janelia (Ashburn, United States) LING PATHWAYS Lin Hui Chang (1) POS008 (1) University of Massachusetts-Amherst (Amherst, United States) TIA-1 RRM23 BINDING AND RECOGNITION OF TARGET OLIGONUCLEOTIDES Saboora Waris (1), Sofía M García-Mauriño, Andrew Sivakumran, Simone POS016 A Beckham, Fionna E Loughlin, Myriam Gorospe, Irene Díaz-Moreno, COMPUTATIONAL DESIGN OF PHOTO- AND CHEMO-SENSITIVE THERAPEUTIC Mather C.J Wilce, Jaqueline A Wilce ENZYMES (1) Monash University (Melbourne, Australia) Sagar Khare (1), Kristin Blacklock, Brahm Yachnin (1) Rutgers The State University of New Jersey (Piscataway, United States)

86 87 #PS32 POS023 Posters NE-CAT: CRYSTALLOGRAPHY BEAMLINES FOR CHALLENGING STRUCTURAL BIOLOGY RESEARCH POS017 Kay Perry (1), Surajit Banerjee, Malcolm Capel, Igor Kourinov, Ed Lynch, Frank FACTORS STABILIZING THE S48P MUTANT OF RIBONUCLEASE SA Murphy, David Neau, Kanagalaghatta Rajashankar, Cyntia Salbego. Jona- Shubhangi Gupta (1), Y U Sasidhar than Schuermann, Nayaranasami Sukumar, James Withrow, Steven Ealick (1) Indian Institute of Technology Bombay (Mumbai, India) (1) Cornell University/NE-CAT (Lemont, United States)

POS018 POS024 MONOMER/TETRAMER EQUILIBRIUM OF -SYNUCLEIN IN SOLUTION AND ITS THE EFFECT OF ANTIBODY F11.2.32 BINDING ON THE ACTIVITY OF HIV-1 INFLUENCE ON FIBRIL FORMATION PROTEASE Yuji Goto (1), Cesar Aguirre, Kensuke Ikenaka, Masatomo So, Keiichi Ya- Apoorva Badaya (1), Yellamraju U. Sasidhar maguchi, Hideki Mochizuki (1) Department of Chemistry, Indian Institute of Technology Bombay, (1) Osaka University, Institute for Protein Researchr (Suita, Japan) Powai, Mumbai 400076 (Mumbai, India)

POS019 POS025 THE EVOLUTION OF DYNAMIC AMINO ACID INTERACTION NETWORKS AMINOACYL-TRNA SYNTHETASES: INVESTIGATIONS OF SPECIFICITY FOR AROUND THE CATALYTIC CYCLE OF A TRYPTOPHAN SYNTHASE APPLICATION IN PROXIMAX / SYNTHETIC BIOLOGY David Boehr (1), Kathleen O'Rourke, Rebecca D'Amico, Debashish Sahu Marta M. Ferreira Amaral (1), Laura Frigotto, Christopher G. Ullman, Guy (1) Pennsylvania State University (University Park, United States) Hermans, Anna V. Hine (1) Aston University (Birmingham, United Kingdom) POS020 UBIQUITIN RECEPTORS MEDIATE PROTEASOMAL PROCESSIVITY POS026 Daniel Kraut (1), Mary Cundiff, Christina Hurley, Jeremy Wong, Eden Reich- DISCOVERY AND CHARACTERIZATION OF MICROPROTEINS ard, Nicholas Nassif Sarah Slavoff (1) (1) Villanova University (Villanvoa, United States) (1) Yale University (West Haven, United States)

POS021 POS027 COILED COILS AS STRUCTURAL BUILDING BLOCKS: A SEQUENCE-BASED THE CRYSTAL STRUCTURE OF HUMAN GELSOLIN D187N PATHOLOGICAL VARIANT APPROACH TOWARDS TUNING COILED COIL MECHANICS Amal Hassan (1), Francesco Boni, Mario Milani, Eloise Mastrangelo, Alber- Patricia Lopez Garcia (1), Melis Göktas, Kerstin G. Blank to Barbiroli, Matteo de Rosa (1) Max Planck Institute of Colloids and Interfaces (Potsdam, Germany) (1) University of Milano (Milan, Italy)

POS022 POS028 IDENTIFYING SUBSTRATE-SMALL HEAT SHOCK PROTEIN INTERACTIONS UNNATURAL AMINO ACID MUTAGENESIS AND BIOORTHOGONAL CHEMISTRY Kathryn McMenimen (1), Emily Gliniewicz, Helen Campbell, Lilong Teng, ENABLE SINGLE-CELL ANALYSIS OF CLASS B GPCR DYNAMICS IN LIVE CELLS Chenwei Wang Qing Lin (1) (1) Mount Holyoke College (South Hadley, United States) (1) SUNY Buffalo (Buffalo, United States)

88 89 #PS32 POS035 Posters TRANSLOCON DECLOGGER STE24/ZMPSTE24 RESCUES IAPP-OLIGOMER INDUCED PROTEOTOXICITY POS029 Can Kayatekin (1), Audra Amasino, Giorgio Gaglia, Jason Flannick, Julia TARGETING PTX3 CAN PREVENT DRUG-RESISTANT CANCER PROGRESSION Bonner, Saranna Fanning, Priyanka Narayan, M. Inmaculada Barrasa, Ju-Ming Wang (1), Jhih-Ying Chi, Yu-Wei Hsiao, Chien-Feng Li, Yu-Chih Lo, David Pincus, Dirk Landgraf, Justin Nelson, Michael Constanzo, Chad Myers, Zu-Yau Lin, Jhen-Yi Hong, Yang-Ming Liu, Xiu Han, Shao-Ming Wang, Charles Boone, Jose Florez, Susan Lindquist Ben-Kuen Chen, Kelvin K. Tsai (1) Whitehead Institute for Biomedical Research (Cambridge, United (1) NCKU Department of Biotechnology and Bioindustry Sciences (Tainan, States) Taiwan) POS036 POS030 STRUCTURAL BASIS OF SERUM AMYLOID A INTERACTIONS WITH LIPIDS AND THE CONSTRUCTION OF A HIGHLY SENSITIVE, MODULAR BIOSENSOR FUNCTIONAL IMPLICATIONS IN LIPID CLEARANCE AND AMYLOID FORMATION Nadia Abascal (1), Lynne Regan Nicholas Frame (1), Shobini Jayaraman, Olga Gursky (1) Yale University (East Haven, United States) (1) Boston University School of Medicine, Department of Physiology & Biophysics (Boston, United States) POS031 STRUCTURAL REMODELING OF HIGH-DENSITY LIPOPROTEINS IN PATIENTS POS037 WITH DIABETES MELLITUS PDB-WIDE IDENTIFICATION OF BIOLOGICAL ASSEMBLIES FROM CONSERVED Clive Baveghems (1), Shobini Jayaraman, Olga Gursky QUATERNARY STRUCTURE GEOMETRY (1) Department of Physiology and Biophysics, Boston University School of Sucharita Dey (1), David Ritchie, Emmanuel Levy Medicine (Boston, United States) (1) Weizmann Institute of Science (Rehovot, Israel)

POS032 POS038 INTERPLAY BETWEEN ACTIVE AND INACTIVE STATES IN LIGHT-SENSING HISTIDINE ENGINEERING SYNTHETIC ANTIBODIES AS PROBES TO DISSECT THE ENERGET- KINASE EL346 IC CONTRIBUTIONS OF CONFORMATIONAL CHANGES IN PROTEINS UPON Igor Dikiy (1), Uthama Edupuganti, Rinat Abzalimov, Peter Borbat, Jack LIGAND BINDING Freed, Kevin Gardner Somnath Mukherjee (1), Dionne Griffi n, James Horn, Shahir Rizk, Malgorza- (1) CUNY Advanced Science Research Center (New York, United States); ta Nocula-Lugowska, Anthony Kossiakoff (1) University of Chicago (Chicago, United States) POS033 SIMULATING THE DYNAMICS OF GTPASES ON THE RIBOSOME POS039 Paul Whitford (1) STRUCTURAL TRANSITIONS IN CONSERVED, ORDERED BECLIN 1 DOMAINS (1) Northeastern University (Boston, United States) ESSENTIAL TO REGULATING AUTOPHAGY Sangita Sinha (1), Karen Glover, Yue Li, Shreya Mukhopadhyay, Srinivas POS034 Chakravarthy, Christopher Colbert RECONSTITUTION OF MAMMALIAN HDAC-CATALYZED DEACYLATION REAC- (1) North Dakota State University (Fargo, United States) TIONS IN BACTERIA Eyal Arbely (1) POS040 (1) Ben-Gurion University of the Negev, Department of Chemistry and the AN ACTIVE ENZYME CLUSTER INSIDE A PROTEIN-GOLD CONJUGATED SHELL: National Institute for Biotechnology in the Negev (Beer Sheva, Israel) FABRICATION OF A HYBRID ENZYME-INORGANIC CATALYST SYSTEM Sharmistha Sinha (1), Naimat Bari, Jagadish Hazra, Ankush Garg, Aashish Bhatt, Md. Ehesan Ali (1) Institute of Nano Science and Technology (Mohali, India) 90 91 POS049 #PS32 Posters PHASE TRANSITION IN TRANSCRIPTIONAL REGULATION Huabin Zhou (1), Luhua Lai (1) Peking University (Beijing, China) POS041 SAXS CONFIRMS THAT FRET DYES PROMOTE COLLAPSE OF AN OTHERWISE POS050 DISORDERED PROTEIN DECIPHERING THE MODE OF REGULATION AND FUNCTIONAL REDUNDANCY Tobin Sosnick (1), Joshua Riback, Micayla Bowman, Adam Zmyslowski, OF HTRA4 – A SERINE PROTEASE IMPLICATED IN THE CELL DEATH PATHWAY Kevin Plaxco, Patricia Clark Raghupathi Kummari (1), Dr. Kakoli Bose (1) University of Chicago (CHICAGO, United States) (1) PhD scholar at ACTREC, TATA Hospital, HBNI, Kharghar. (Mumbai, India)

POS042 POS051 RE-TARGETING A BACTERIAL ASSASSIN: ENGINEERING PLYC SPECIFICITY COMPARISON OF CRYSTAL AND CRYOEM STRUCTURES OF HSP104 AND USING DIRECTED EVOLUTION CLPB DISAGGREGASES Sebastian Broendum (1), Ben Clifton, Blake Riley, Colin Jackson, Ashley Andrzej Joachimiak (1), Karolina Michalska, Kaiming Zhang, Zachary Buckle, Sheena McGowan March, Catherine Hatzos-Skintges, Grigore Pintilie, Lance Bigelow, Laura (1) Monash University, Department of Biochemistry and Molecular Biology Castellano, Leanne Miles, Meredith Jackrel, Edward Chuang, Robert (Monash, Australia) Jedrzejczak, James Shorter, Wah Chiu (1) Argonne National Laboratory/University of Chicago (Argonne, United POS043 States) STRUCTURE ANALYSIS OF EMERICELLIPSIN A, A NOVEL PEPTAIBOL SECRETED BY EXTREMOPHILIC FUNGUS EMERICELLOPSIS ALKALINA BILANENKO & GEORGIEVA POS052 Eugene Rogozhin (1), Alexey Vasilchenko, Anna Baranova, Konstantin Mi- CONTACT DEPENDENT GROWTH INHIBITION TOXIN UTILIZES ELONGATION neev, Marina Georgieva, Alexander Kul'ko, Mikhail Krasheninnikov, Alexey FACTOR TU FOR ACTIVITY Lyundup, Yaroslav Andreev, Vera Sadykova Karolina Michalska (1), Grant Gucinski, Fernando Garza-Sánchez, Parker (1) Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry Russian Academy Johnson, Lucy Stols, William Eschenfeldt, Gyorgy Babnigg, David Low, of Sciences (Moscow, Russia) Celia Goulding, Christopher Hayes, Andrzej Joachimiak (1) Argonne National Laboratory (Lemont, United States) POS044 A COMPUTATIONAL STUDY OF THE ADDITIVITY OF BINDING FREE ENERGY IN POS053 PROTEIN-PROTEIN COMPLEXES UPON DOUBLE MUTATION A THREONINE ZIPPER THAT MEDIATES PROTEIN-PROTEIN INTERACTIONS: Sherlyn Jemimah (1), Michael Gromiha STRUCTURE AND PREDICTION (1) Indian Institute of Technology Madras (Chennai, India) Curran Oi (1), John Treado, Christopher Lim, Kirsten Knecht, Yong Xiong, Corey O'Hern, Lynne Regan POS045 (1) Yale University (New Haven, United States) ITACONATE INHIBITS THE NF-ΚB SIGNALING PATHWAY ACTIVATION Yalei Zhang (1), Luhua Lai POS054 (1) Peking university (Beijing, China) BROAD MUTATIONAL SCANNING ACROSS PROTEIN FAMILIES Calin Plesa (1), Angus Sidore, Nathan Lubock, Di Zhang, Sriram Kosuri POS048 (1) UCLA (Los Angeles, United States) RATIONAL DESIGN OF A CADMIUM RESPONSIVE LIVING SENSOR Hengyi Li (1), Changsheng Zhang, Luhua Lai POS055 (1) Peking University (Beijing, China) MASS SPECTROMETRIC CHARACTERIZATION OF A RECOMBINANT ‘TWO-TAR- GET’ FUSION PROTEIN Siddharth Bhoraskar (1), Charan Kumar Ramineni, Jin Xu 92 (1) University of Massachusetts Lowell (Lowell, United States) 93 #PS32 Posters POS062 DESIGN OF MODULAR SWITCHES FOR ALLOSTERIC CONTROL OVER PROTEIN KINASES AND PROTEIN PHOSPHATASES POS056 Matthew Bienick (1) DISCOVERING ENZYMES FOR SYNTHESIS OF ANTIBIOTICS RELATED TO (1) University of Arizona (Tucson, United States) KANOSAMINE Theerawat Prasertanan (1), David R.J. Palmer, David A.R. Sanders POS063 (1) University of Saskatchewan (Saskatoon, Canada) APPLICATION OF MALDI IMAGING MS FOR RELATIVE QUANTITATION OF POST-TRANSLATIONAL MODIFICATIONS OF AMYLOID-Β PEPTIDE POS057 Stanislav Pekov (1), Daniil Ivanov, Maria Indeykina, Alexey Kononikhin, Igor STRUCTURAL UNIQUENESS AND SPECIFIC RECOGNITION OF TRANSLATION Popov, Eugene (Evgeny) Nikolaev INITIATION FACTOR 1 TO THE 30S RIBOSOMAL SUBUNIT IN PSEUDOMONAS (1) Moscow Institute of Physics and Technology (Moscow, Russia) AERUGINOSA PROTEIN SYNTHESIS Yonghong Zhang (1), James Bulllard POS064 (1) The University of Texas Rio Grande Valley (Edinburg, United States) COMBINING STRUCTURE AND DYNAMICS TO UNDERSTAND USP7 FUNCTION Gabrielle Valles (1) POS058 (1) UConn Health (Farmington, United States) FACILITATING THE EFFECT OF PENTRAXIN 3 ON SHRIMP ALLERGIC RESPONSES IN IGE-ACTIVATED MAST CELLS POS065 Jyun-Yi Du (1), Ju-Ming Wang INTERROGATING THE SELECTIVITY OF PROTEASOME ASSOCIATED DEUBIQUITINASE (1) NCKU Department of Biotechnology and Bioindustry Sciences (Tainan, UCH37 AND DEVELOPING INHIBITORS USING HIGH THROUGHPUT SCREENING Taiwan) Jiale Du (1) (1) Umass-Amherst (Amherst, United States) POS059 SINGULAR VALUE DECOMPOSITION FOR THE CORRELATION OF ATOMIC POS066 FLUCTUATIONS WITH ARBITRARY ANGLE OPTIMIZATION OF THE BLIP-II INTERACTION WITH PBP2A AS A PROTEIN-BASED Miao Yu (1), Zhirong Liu (1) THERAPEUTIC OPTION FOR MRSA (1) Peking University (Beijing, China) David Boragine (1), Carolyn Adamski, Shrenik Mehta, Timothy Palzkill (1) Baylor College of Medicine (Houston, United States) POS060 ELUCIDATION OF AN EXPANDED AGGREGATION-PRONE CONFORMATION POS067 OF FAB USING SAXS, MD SIMULATIONS AND SMFRET INTERACTIONS OF THE E. COLI Β-CLAMP AND Γ-CLAMP LOADER COMPLEX Nuria Codina (1), Paul Dalby, Stephen Perkins, David Hilton, Cheng Zhang DURING THE CLAMP LOADING PROCESS (1) University College London (London, United Kingdom) Socheata Lim (1) (1) University of Connecticut Health (Danbury, United States) POS061 SYNTHETIC TRANSPORT SYSTEMS IN BACTERIA POS068 Tilmann Kuenzl (1), Elisabetta Groaz, Piet Herdewijn, Philippe Marlière, SPECIFIC ACTIVATION OF THE ERYTHROPOIETIN RECEPTOR BY ULTRA-SIMPLE Sven Panke ARTIFICIAL TRANSMEMBRANE PROTEINS (1) ETH Zurich (Basel, Switzerland) Li He (1), Rachel Strodel, Emily Cohen, Erin Heim, Daniel DiMaio (1) Yale University (New Haven, United States)

94 95 #PS32 POS076 Posters QUANTIFYING NUCLEATION IN VIVO REVEALS THE PHYSICAL BASIS OF PRI- ON-LIKE PHASE BEHAVIOR Randal Halfmann (1), Tarique Khan, Tejbir Kandola, Jianzheng Wu, Ellen POS069 Ketter, Shriram Venkatesan, Jeffrey Lange, Alejandro Rodriguez-Gama, A BIOPHYSICAL STUDY OF THE INTERACTION OF THE CARBOXY-TERMINUS OF Andrew Box, Jay Unruh, Malcolm Cook HPV L2 MINOR CAPSID PROTEIN WITH MEMBRANES (1) Stowers Institute for Medical Research (Kansas City, United States) Mohan Pereira (1), Gabriel Silva, Daniel DiMaio (1) Yale Uuniversity (New Haven, United States) POS077 TOWARDS ACCURATE AND RELIABLE PROTEIN STRUCTURE PREDICTION WITH POS070 X-RAY SCATTERING MOLECULAR MECHANISM OF A VOLTAGE-DEPENDENT, PROTON-COUPLED Susan Tsutakawa (1), Tadeusz Ogorzalek, Greg Hura, Andriy Kryshtafo- TRANSITION METAL TRANSPORTER vych, Krzysztof Fidelis, John Tainer Aaron Bozzi (1), Christina ZImanyi, Lukas Bane, Rachelle Gaudet (1) LBNL (Berkeley, United States) (1) Harvard University (Cambridge, United States) POS078 POS071 TARDIGRADE DISORDERED PROTEINS PROTECT ENZYMES AGAINST DESICCATION FUNCTIONAL CHARACTERIZATION OF THE CYCLIC NUCLEOTIDE-GATED AND RESURRECT DESICCATION-DAMAGED ENZYMES CHANNEL STHK Samantha Piszkiewicz (1), Owen Warmuth, Aakash Mehta, Kenny Nguyen, Philipp Schmidpeter (1), Xiaolong Gao, Jan Rheinberger, Crina Nimigean Ashlee Propst, Gary Pielak (1) Weill Cornell Medicine (New York, United States) (1) UNC Chapel Hill (Chapel Hill, United States)

POS072 POS079 STRUCTURE AND REGULATION OF E. COLI CYCLOPROPANE FATTY ACID SYNTHASE COMPENSATORY MUTATIONS AND DISEASE IN HUMAN GLUTAMINE SYNTHETASE Sanjay B. Hari (1), Robert A. Grant, Robert T. Sauer Erin Thompson (1), James Fraser (1) Massachusetts Institute of Technology (Cambridge, United States) (1) UCSF (San Francisco, United States)

POS073 POS080 KNOB-SOCKET PREDICTIONS OF ALPHA-HELICAL STABILITY STRUCTURAL AND FUNCTIONAL STUDIES OF E.COLI GUANINE DEAMINASE Taylor Rabara (1), Melina Huey, Danielle MacArt, Hyun Joo, Jerry Tsai Roger Shek (1), Jarrod French (1) University of the Pacifi c (Stockton, United States) (1) Stony Brook University (Stony Brook, United States)

POS074 POS081 DISULFIDE BONDS AND HOW THEY CAUSE PROTEIN AGGREGATION: PERSPECTIVES THE AUTOPHAGY-RELATED BECLIN-1 PROTEIN REQUIRES BOTH THE COILED-COIL FROM NMR, MD MODELING AND CELL CULTURE EXPERIMENTS AND BARA DOMAINS TO FORM A HOMODIMER WITH SUB-MICROMOLAR AFFINITY Nikolai Skrynnikov (1), Sevastyan Rabdano, Sergei Izmailov, Irina Tyuryae- Matthew Ranaghan (1), Michael Durney, Michael Mesleh, Patrick McCa- va, Dmitry Luzik, Olga Rogacheva, Olga Lyublinskaya, Ivan Podkorytov rren, Colin Garvie, Douglas Daniels, Kimberly Carey, Adam Skepner, Beth (1) Laboratory of Biomolecular NMR, St. Petersburg State University / De- Levine, Jose Perez partment of Chemistry, Purdue University (St. Petersburg, Russia) (1) The Broad Institute of MIT and Harvard (Cambridge, United States)

POS075 POS082 CONFORMATIONAL PLASTICITY OF LATE EMBRYOGENESIS ABUNDANT (LEA) MECHANISM AND CONSEQUENCES OF REENTRANT PHASE TRANSITION OF PROTEINS INTRINSICALLY DISORDERED PROTEINS Brett Janis (1), Michael Menze Priya Banerjee (1), Ibraheem Alshareedah (1) University of Louisville (Louisville, United States) (1) University at Buffalo, SUNY (Buffalo, United States) 96 97 #PS32 POS090 Posters ENGINEERED MONO- AND MULTI-VALENT REPEAT-PROTEIN ARRAYS TO IN- HIBIT ONCOGENIC TANKYRASES POS083 Aurora Diamante (1), Albert Perez-Riba, Marc de la Roche, Laura Itzhaki ACETYL-GROUP SENSING THROUGH MODULATION OF CONFORMATIONAL (1) University of Cambridge, Department of Pharmacology (Cambridge, DYNAMICS IN AN ARYLALKYLAMINE N-ACETYLTRANSFERASE United Kingdom) Adam Aboalroub (1) (1) Graduate Research Assistant (Tampa, United States) POS091 CRYSTAL STRUCTURES OF AFLATOXIN-OXIDASE FROM ARMILLARIELLA TABES- POS084 CENS REVEAL A DUAL ACTIVITY ENZYME STRUCTURAL BASIS OF HIV-1 INHIBITION BY THE NUCLEOTIDE-COMPETING Tingting Xu (1), Xie Chunfang, Dongsheng Yao, Cong-Zhao Zhou, Jinsong REVERSE TRANSCRIPTASE INHIBITOR INDOLOPYRIDONE-1 (INDOPY-1) Liu Francesc X. Ruiz (1), Anthony Hoang, Kalyan Das, Eddy Arnold (1) Guangzhou Institutes of Biomedicine and Health,Chinese Academy of (1) Center for Advanced Biotechnology and Medicine, and Department Sciences (Guangzhou, China) of Chemistry and Chemical Biology, Rutgers University (Piscataway, United States) POS092 COMPUTATIONAL TOOLS FOR DEEP MUTATIONAL SCANNING POS085 Alan F Rubin (1), Daniel Esposito, Jochen Weile, Frederick P Roth, Douglas CISD2: AN UNNOTICED REGULATOR OF MITOCHONDRIA PERFORMANCE? M Fowler, Anthony T Papenfuss Robert Skolik (1), Werner Geldenhuys, Mary Konkle, Michael Menze (1) The Walter and Eliza Hall Institute of Medical Research (Parkville, Aus- (1) University of Louisville (Louisville, United States) tralia) POS086 POS094 HIGH THROUGHPUT MACROMOLECULAR STRUCTURE IN SOLUTION USING SNX16 REGULATES THE RECYCLING OF E-CADHERIN THROUGH A UNIQUE SMALL ANGLE X-RAY SCATTERING (SAXS) MECHANISM OF COORDINATED MEMBRANE AND CARGO BINDING Tad Ogorzalek (1), Scott Classen, Susan Tsutakawa, Greg Hura, John Jinxin Xu (1), Leilei Zhang, Yinghua Ye, Yongli Shan, Chanjuan Wan, Jun- Tainer feng Wang, Duanqing Pei, Xiaodong Shu, Jinsong Liu (1) Lawrence Berkeley National Labs (Berkeley, United States) (1) Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences (Guangzhou, China) POS087 CONSTRUCTION OF SUPERCHARGED GFP-BASED DUAL SPLIT REPORTER PROTEIN POS095 Zene Matsuda (1), Jiping Song ,Yasushi Kawaguchi, Jun-ichiro Inoue PEPTIDE GRAFTING INTO A REPEAT PROTEIN IMPARTS LOW NANOMOLAR (1) Research Center for Asian Infectious Diseases, Institute of Medical AFFINITY FOR KEAP1 Science, the University of Tokyo (Minato-ku, Japan) Sarah Madden (1), Albert Perez-Riba, Laura Itzhaki (1) Department of Pharmacology, University of Cambridge (Cambridge, POS089 United Kingdom) DRIVING IMMUNE RESPONSES WITH SYNTHETIC PROTEINS - DEVELOPMENT OF DE NOVO DESIGNED IMMUNOGENS TO ELICIT RESPIRATORY SYNCYTIAL POS096 VIRUS NEUTRALIZING ANTIBODIES MANIPULATING THE ENERGY LANDSCAPES OF BETA-LACTAMASE ENZYMES Fabian Sesterhenn (1), Che Yang, Jaume Bonet, Marie Galloux, Xiaolin Miranda Villanueva (1), Kathryn Hart Wen, Johannes Thomas Cramer, Patricia Corthésy Henrioud, Stéphane (1) Williams College (Williamstown, United States) Rosset, Jean-François Éléouët, Ted Jardetzky, Thomas Krey, Sabine Riffault, Bruno Emanuel Correia (1) Institute of Bioengineering, École Polytechnique Fédérale de Lausanne (Lausanne, Switzerland) 98 99 #PS32 POS105 Posters INTERDOMAIN LINKER REGIONS OF A AAA+ PROTEIN UNFOLDASE MEDIATE EFFICIENT INTERSUBUNIT COMMUNICATION POS097 Tristan Bell (1), Tania Baker, Robert Sauer SURVIVAL OF THE FITTEST: USING COMPETITION ASSAYS TO ASSESS THE IM- (1) MIT (Cambridge, United States) PACT OF PROTEIN STABILITY ON ORGANISMAL FITNESS Cynthia Okoye (1), Kathryn Hart POS107 (1) Williams College (Williamstown, United States) STRUCTURE, STABILITY AND SPECIFICITY OF THE BINDING OF SSDNA AND SSRNA WITH PROTEINS POS098 Arumay Pal (1), Yaakov Levy MACROMOLECULAR CROWDING EFFECTS ON BUFORIN II - NUCLEIC ACID (1) Weizmann Institute of Science (Rehovot, Israel) BINDING: A COMPARATIVE COMPUTATIONAL STUDY USING MULTIPLE MODELS Carla Perez (1), Donald Elmore, Mala Radhakrishnan POS108 (1) Department of Chemistry, Wellesley College (Wellesley, United States) ENGINEERING A RATIOMETRIC FLUORESCENT PROTEIN SENSOR OF EXTRA- CELLULAR ATP TO STUDY PURINERGIC SIGNALING POS099 Dan Cholger (1), Jason Conley, Stephan Valentino CHARACTERIZING SUBUNIT EXCHANGE IN CAMKII ISOFORMS (1) Purdue University (West Lafayette, United States) Ana Torres-Ocampo (1), Margaret Stratton (1) University of Massachusetts-Amherst (Amherst, United States) POS109 DEEP MUTATIONAL SCANNING OF THE BETA-2 ADRENERGIC RECEPTOR POS101 Eric Jones (1), Nathan Lubock, Daniel Cancilla, Megan Satyadi, Rishi DEVELOPING AND OPTIMIZING METHODOLOGIES TO DIFFERENTIATE STREP- Jajoo, Sriram Kosuri TOCOCCUS MUTANS AMYLOIDS FROM MONOMERS (1) UCLA (Los Angeles, United States) Ana Barran (1), Joanna R Long, L. Jeannine Brady (1) Department of Oral Biology, University of Florida (Gainesville, United States) POS110 STRUCTURAL DYNAMICS OF BLUE LIGHT SENSITIVE BACTERIAL PHOTORECEP- POS102 TOR BLSA CONSERVED ASYMMETRY UNDERPINS HOMODIMERIZATION OF DICER-AS- Iva Chitrakar (1), Jarrod French SOCIATED DOUBLE-STRANDED RNA-BINDING PROTEINS (1) Stony Brook University (Stony Brook, United States) Michael Plevin (1), Clément Dégut, Alex Heyam, Claire Coupland, Ruth Haley, Leonhard Jakob, Gunter Meister, Dimitris Lagos POS111 (1) University of York (York, United Kingdom) HIGH-DENSITY CHEMICAL CROSS-LINKING FOR MODELING PROTEIN INTER- ACTIONS POS103 Julian Mintseris (1), Steve Gygi (1) STRUCTURAL INSIGHTS INTO CRISPR AND ANTI-CRISPR SYSTEMS FOR PRECISE (1) Harvard Medical School (Boston, United States) GENOME EDITING Fuguo Jiang (1), Junjie Liu, Eva Nogales, Joseph Bondy-Denomy, Jennifer POS112 Doudna SIGNALING-RELATED MOBILITY CHANGES IN CHEMOTAXIS RECEPTORS (1) UC Berkeley (Berkeley, United States) Maryam Kashefi (1), Lynmarie Thompson (1) Department of Chemistry, University of Massachusetts Amhesrt (Am- POS104 herst, United States) UNCOVERING THE ROLE OF PROTEASOME-BOUND UCH37 Sean Crowe (1), Kirandeep Deol, Jiale Du, Eric Strieter (1) University of Massachusetts Amherst (Amherst, United States) 100 101 POS120 #PS32 Posters INSIGHTS INTO THE HOMODIMERIC INTERFACE OF HUMAN GALECTIN-7: FROM STRUCTURAL AND BIOPHYSICAL CHARACTERIZATION TO IMMUNO- POS113 SUPPRESSIVE ACTIVITY ASSAYS HYSTERESIS IN HUMAN UDP-GLUCOSE DEHYDROGENASE REQUIRES REPACKING Ngoc Thu Hang Pham (1), Myriam Letourneau, Marie-Aude Pinoteau, Mar- OF THE PROTEIN CORE lene Fortier, Jacinthe Gagnon, Philippe Egesborg, David Chatenet, Yves Nathaniel Beattie (1), Brittany Pioso, Andrew Sidlo, Nicholas Keul, Zachary Wood St-Pierre, Charles Calmettes, Nicolas Doucet (1) University of Georgia (Athens, United States) (1) INRS - Institut Armand-Frappier, Universite Du Quebec (Laval, Canada) POS114 POS121 CREATINE KINASE POST-TRANSLATIONAL MODIFICATION IN METABOLIC A NOVEL MODE OF PEPTIDE PRESENTATION OF MAJOR HISTOCOMPATIBILITY DEPRESSION COMPLEX CLASS I Christine Childers (1), Kenneth Storey Xiaolong Li (1), Pedro Lamothe, Bruce Walker, Jia-huai Wang (1) Carleton University (ottawa, Canada) (1) Dana-Farber Cancer Institute, Harvard Medical School (Boston, United States) POS115 INTERROGATING A MULTIDRUG EFFLUX MEMBRANE PROTEIN TRANSPORTER POS122 INVOLVED IN BACTERIAL ANTIBIOTIC RESISTANCE USING STRUCTURAL MASS COMPLETING THE STRUCTURE OF A MULTI-COMPONENT VIRAL GENOME SPECTROMETRY PACKAGING MOTOR Zainab Ahdash (1), Eamonn Reading, Argyris Politis Bryon Mahler (1), Huzhang Mao, Erik Dill, Tianzhi Wang, Marc Morais (1) King's College London (London, United Kingdom) (1) Sealy Center for Structural Biology and Molecular Biophysics, Depart- ment of Biochemistry and Molecular Biology, University of Texas Medical POS116 Branch (Galveston, United States) INTRINSICALLY DISORDERED SEGMENTS CAN TUNE PROTEIN FUNCTION Zachary Wood (1), Nicholas Keul , Krishnadev Oruganty, Elizabeth Berg- POS123 man, Nathaniel Beattie, Weston McDonald, Renuka Kadirvelraj, Michael DEVELOPMENT OF A BIOMIMETIC SMALL MOLECULE BASED AFFINITY PURIFICA- Gross, Robert Phillips, Stephen Harvey TION FOR ALPHA-GALACTOSIDASE A: RESEARCH TO COMMERCIAL (1) University of Georgia (Athens, United States) Brian Dwyer (1) (1) Shire (Lexington, United States) POS117 STRUCTURAL CHARACTERIZATION OF HUMAN URIDINE MONOPHOSPHATE POS124 SYNTHASE (UMPS) AND ITS SPATIO-TEMPORAL LOCALIZATION IN CELLS A SINGLE N-TERMINAL PHOSPHOMIMIC DISRUPTS TDP-43 POLYMERIZATION, Deborah Kim-Holzapfel (1), Jarrod French PHASE SEPARATION AND RNA SPLICING (1) Stony Brook University (Stony Brook, United States) Ailin Wang (1) (1) Brown University (Providence, United States) POS118 COLLAGEN ARCHITECTURE REGULATES THE SPECIFICITY OF INTERACTIONS POS126 WITH ITS RECEPTORS UBIQUITIN VARIANTS WITH IMPROVED AFFINITY TARGETING PARKIN E3-LIGASE Cody Hoop (1), Jie Zhu, David Case, Jean Baum Suchithra Guntur (1), Jonas Michaelis, Christian Münch, Koraljka Husnjak and (1) Rutgers University (Piscataway, United States) Andreas Ernst (1) Institute of Biochemistry II, Goethe-University, Faculty of Medicine, Theo- POS119 dor-Stern-Kai 7, 60590 Frankfurt, Germany BINDING OF LIGANDS TO MITOCHONDRIAL CISD PROTEINS Ryan Napier (1), Robert Skolik, Mary Konkle, Michael Menze) (1) University of Louisville, Department of Biology (Austin, United States) 102 103 #PS32 POS135 PH-DEPENDENT STRUCTURE AND HYDROGEN-BOND DYNAMICS OF M2 PRO- Posters TON CHANNEL EMBEDDED IN SUPPORTED LIPID BILAYERS REVEALED BY 2D IR POS127 Nam Hyeong Kim (1), William DeGrado, Yung Sam Kim, Yong Ho Kim LOSS OF PROTEIN STABILITY UNDERLIES MANY PATHOGENIC VARIANTS (1) Sungkyunkwan University (Suwon-si, South Korea) Amelie Stein (1), Maher M Kassem, Amanda B Abildgaard, Rasmus Hart- mann-Petersen, Kresten Lindorff-Larsen POS136 (1) Linderstrøm-Lang Centre for Protein Science, University of Copenhagen ASSESSING THE ABILITY OF FOOD PROTEIN NANOFIBRILS TO CROSS-SEED (Copenhagen N, Denmark) AMYLOID FORMATION OF RELATED HUMAN PROTEINS Lida Rahimi Araghi (1), Tong Zhang, Bingqian Xu, Derek Dee POS128 (1) University Of Georgia (Athens, United States) THE PROTONATION OF A BURIED ACID CONTRIBUTES TO THE COST OF THE ALLOSTERIC TRANSITION IN HUMAN UDP-GLUCOSE DEHYDROGENASE POS137 Phillip Gross (1), Jeffery Fallah, Lauren Ellis, Zachary Wood MAPPING ENZYME MOTIONS IN REAL TIME USING TIME-RESOLVED TEMPERA- (1) University of Georgia (Athens, United States) TURE-JUMP X-RAY CRYSTALLOGRAPHY AND SAXS/WAXS Michael Thompson (1), Alexander Wolff, Benjamin Barad, Eriko Nango, Mi- POS129 noru Kubo, Michihiro Sugahara, Hynu Sun Cho, Aaron Brewster, Iris Young, GENETICALLY ENCODED P19-SENSOR PROTEIN FOR DETECTION AND DELIV- Friedrich Schotte, Rie Tanaka, Kensuke Tono, So Iwata, Nicholas Sauter, ERY OF SMALL RNAS Philip Anfi nrud, James Fraser Noreen Ahmed (1), Nadine Ahmed, Dana Foss, John Pezacki (1) University of California, San Francisco (San Francisco, United States) (1) University of Ottawa (Ottawa, Canada) POS138 POS131 DE NOVO DESIGN OF Α-AMYLOIDS THAT ASSEMBLE IN VITRO AND IN VIVO TOWARDS NEW UO22+ BIOSENSORS BASED ON SUPER URANYL-BINDING PROTEIN Shao-Qing Zhang (1), Hai Huang, Junjiao Yang, Huong Kratochvil, Marco Marie Hoarau (1), Xingquan Zou, Zhan Chen, Neil Marsh Lolicato, Xiaokun Shu, Lijun Liu, William DeGrado (1) University of Michigan (Ann Arbor, United States) (1) UCSF (San Francisco, United States)

POS132 POS139 DESIGN AND DYNAMICS OF BIOMOLECULAR PEPTIDE ASSEMBLY ON SOLID EFFECTS OF PATHOLOGICAL MUTATIONS ON THE PRION-LIKE POLYMERIZA- SUBSTRATES TION OF MYD88 Young Hyun No (1), Nam Hyeong Kim, Kilho Eom, Yong Ho Kim Yann Gambin (1) (1) SKKU Advanced Institute of Nanotechnology (SAINT), Sungkyunkwan (1) EMBL Australia - UNSW (Randwick, Australia) University (Suwon, South Korea) POS140 POS133 TUNABLE CHEMISTRY FOR BIOORTHOGONAL LIGATION AND DECOUPLING ENGINEERING CELL-SURFACE SENSORS OF EXTRACELLULAR ATP OF PROTEIN CONJUGATES Mathew Tantama (1), Jason Conley, Daniel Cholger, Stephen Valentino Tak Chio (1), Han Gu, Susan Bane (1) Purdue University (West Lafayette, United States) (1) State University of New York at Binghamton (Binghamton, United States) POS134 MULTICOMPARTMENT REDOX IMAGING WITH FRET RELAY-BASED RED-SHIFT- POS141 ED ROGFP THE SHIFTING INTERACTOME OF ALPHA-SYNUCLEIN ALONG ITS AGGREGA- Mathew Tantama (1), Jacob Norley, Saranya Radhakrishnan, Nathan TION PATHWAY LeRoy, Sarah Doan Emma Sierecki (1), James Brown, Andre Leitao, Alexandre Chappard, (1) Purdue University (West Lafayette, United States) Yann Gambin 104 (1) University of New South Wales (Randwick, Australia) 105 POS148 #PS32 FIPRONIL-INDUCED PROTEOSTASIS STRESS IN SH-SY5Y CELLS Posters N. Monique Paricharttanakul (1), Theetat Ruangjaroon, Daranee Chok- POS142 chaichamnankit, Chantragan Srisomsap, Jisnuson Svasti FLUORESCENT SENSORS FOR DETECTION OF PROTEIN CARBONYLATION (1) Laboratory of Biochemistry, Chulabhorn Research Institute (Bangkok, Kamalika Mukherjee (1), Tak Chio, Dan Sackett, Susan Bane Thailand) (1) Massachusetts General Hospital, Harvard Medical School (Charles- town, United States) POS149 RCSB PROTEIN DATA BANK: SUSTAINING A LIVING DIGITAL DATA RESOURCE POS143 THAT ENABLES BREAKTHROUGHS IN SCIENTIFIC RESEARCH AND BIOMEDICAL ROLE OF PROTEOLYSIS IN THE STRUCTURE AND REMODELING OF HIGH-DEN- EDUCATION SITY LIPOPROTEIN Stephen K. Burley (1), Cole Christie, Jose Duarte, Zukang Feng, Tara Kalro, Shobini Jayaraman (1) John Westbrook, Jasmine Young Christine Zardecki (1) Boston University (Boston, United States) (1) RCSb Protein Data Bank; Rutgers University (Piscataway, United States)

POS144 POS150 MEASURING THE FUNCTIONAL EFFECT OF AMINO ACID SUBSTITUTIONS PRO- CONSERVED COACTIVATOR BINDING MECHANISMS FACILITATE DISCOVERY TEOME-WIDE USING MISTRANSLATION OF ALLOSTERIC SMALL MOLECULES Stephanie Zimmerman (1), Richard Rodriguez-Mias, Bianca Ruiz, Judit Matthew Henley (1), Amanda Peiffer, Andrew Henderson, Nicholas Foster, Villen, Stan Fields Brian Linhares, Zachary Hill, James Wells, Tomasz Cierpicki, Charles Brooks (1) University of Washington Department of Genome Sciences (Seattle, III, Carol Fierke, Anna Mapp United States) (1) University of Michigan (Ann Arbor, United States)

POS145 POS151 RATIONAL DESIGN OF PROTEIN FIBRILS FORMED BY Α-HELICES UNDERSTANDING PROTEIN-PROTEIN INTERACTIONS THROUGH COMPREHEN- Xiangyu Sun (1), Luhua Lai SIVE MAPPING OF BINDING LANDSCAPES (1) Peking University (Beijing, China) Julia Shifman (1), Michael Heyne, Itay Cohen, Yoav Peleg, Jason Shirian, Niv Papo POS146 (1) Hebrew University of Jerusalem (Jerusalem, Israel) LIPID- AND CHOLESTEROL-MEDIATED TIMESCALE-SPECIFIC MODULATION OF MEMBRANE PROTEIN DYNAMICS POS152 Lukas Frey (1), Sebastian Hiller, Roland Riek, Stefan Bibow HOW SOME CRITICAL N- AND C-TERMINAL RESIDUES OF CHAPERONIN GRO- (1) ETH Zurich (Zurich, Switzerland) EL PLAY SIGNIFICANT ROLE IN ITS FOLDING, MULTIMERIC ASSEMBLY AND THERMODYNAMIC STABILITY POS147 Tapan Chaudhuri (1), Sarita Puri DESIGNING PROTEIN POLYHEDRA USING A GENERALIZABLE SYMME- (1) Indian Institute Of Technology Delhi (New Delhi, India) TRY-BASED APPROACH Ajitha Cristie-David (1), Neil Marsh POS153 (1) University of Michigan (Ann Arbor, United States) THE ACTION OF MOLECULAR MACHINES REVEALED BY HX-MS Xiang Ye (1), Leland Mayne, Walter Englander (1) University of Pennsylvania (Philadelphia, United States)

106 107 #PS32 POS162 Posters INTEGRATE STRUCTURAL INFORMATION TO STUDY THE KINETICS OF PRO- TEIN-PROTEIN INTERACTIONS AND PROTEIN COMPLEX ASSEMBLY BY MULTI- POS154 SCALE MODELING UNRAVELING A NEW REGULATORY MECHANISM IN SRC KINASE USING A Yinghao Wu (1) CHEMICAL GENETICS TOOL AND SATURATION MUTAGENESIS (1) Albert Einstein College of Medicine (Bronx, United States) Sujata Chakraborty (1), Ethan Ahler, Emily Dieter, Douglas Fowler, Dustin Maly POS163 (1) Graduate Student (Seattle, United States) ACTIVATION AND REGULATION OF HUMAN ATG3 (HATG3) CONJUGASE IN AUTOPHAGY POS156 Yansheng Ye (1), Erin Tyndall, Zhenyuan Tang, Hong-Gang Wang, Fang Tian CONFORMATIONAL FLEXIBILITY OF PORE LOOP-1 GIVES INSIGHTS INTO SUB- (1) Department of Biochemistry and Molecular Biology, The Pennsylvania STRATE TRANSLOCATION BY AAA+ PROTEASE FTSH State University (Hershey, United States) Matthias Uthoff (1), Ulrich Baumann (1) University of Cologne (Cologne, Germany) POS164 INTEGRATIVE PROTEOMICS OF LARGE, NATIVE AND DYNAMIC CELLULAR POS157 ASSEMBLIES CHARACTERIZATION OF THE B. SUBTILIS DERIVED LIPA AFTER FUSION TO THE Yi Shi (1), Brian Chait HEPB CORE PROTEIN (1) University of Pittsburgh School of Medicine (Pittsburgh, United States) Maanya Gaur (1), Santosh Noronha, Lizhong He (1) Indian Institute of Technology Bombay (Mumbai, India) POS165 A NOVEL EXPERIMENTAL APPROACH FOR TESTING COMPUTATIONAL PROTEIN POS158 DESIGN ENERGETIC AND MECHANISTIC ASPECTS OF EFFECT OF SORBITOL ON HEN Oana-Nicoleta Antonescu (1), Andreas Rasmussen, Nicole A.M. Damm, EGG-WHITE LYSOZYME AND AMINO ACIDS UNDER SALT STRESS Kristoffer E. Johansson, Jakob R. Winther Pooja Meena (1), Nand Kishore (1) Linderstrøm-Lang Centre for Protein Science, Department of Biology, (1) Indian Institute of Technology Bombay (MUMBAI, India) University of Copenhagen (Copenhagen, Denmark)

POS159 POS166 PROTEASES: A NEW MODALITY IN MEDIATING NECROTIC CELL DEATH IN SILICO DETERMINATION OF THE STRUCTURE OF HIV-1 PROTEASE-MONO- Amnon Albeck (1), Ilana Nathan CLONAL ANTIBODY COMPLEX: TOWARDS IDENTIFICATION OF THE MECHA- (1) Bar Ilan University (Ramat GAn, Israel) NISM OF DIMERISATION INHIBITION Suchetana Gupta (1), Sangeetha Balasubramanian, Sanjib Senapati POS160 (1) Department of Biotechnology Indian Institute of Technology Madras 2D-LC APPROACH IN THE PURIFICATION AND CHARACTERIZATION OF PROTEINS (Chennai, India) FROM FENUGREEK (TRIGONELLA FOENUM-GRAECUM) SEEDS Taibah Aldakhil (1), Aftab Ahmed POS167 (1) Chapman University School of Pharmacy (Irvine, United States) THE NEXT TAG: A NOVEL SMALL SOLUBILITY ENHANCER AS A POWERFUL ALTERNATIVE TO MALTOSE-BINDING PROTEIN POS161 Byung Hoon Jo (1), Su Han Wi HIDDEN PARTNERS AND PROTEIN FUNCTION : LESSONS FROM MASSIVE (1) Division of Life Science, Gyeongsang National University (Jinju, South CROSS-DOCKING SIMULATIONS ON PROTEIN-PROTEIN RECOGNITION Korea) Sophie Sacquin-Mora (1), Nathalie Lagarde, Alessandra Carbone (1) Laboratoire de Biochimie Théorique, CNRS UPR9080 (Paris, France) 108 109 #PS32 POS174 CHARACTERIZING THE STRUCTURE OF THE YG BOX OLIGOMER OF THE SPLIC- Posters ING-ASSOCIATED SMN Kaylee Mathews (1), Nicolas L. Fawzi POS168 (1) Brown University (Providence, United States) ELUCIDATING MOLECULAR RECOGNITION ELEMENTS IN A STRUCTURALLY- DIVERGENT ACTIVATOR BINDING DOMAIN POS175 Amanda Peiffer (1), Matthew Henley, Andrew Henderson, Nicholas Foster, FUNCTIONAL AND PATHOLOGICAL DISORDERED PROTEIN PHASE SEPARA- Brian Linhares, Zachary Hill, James Wells, Tomasz Cierpicki, Carol Fierke, TION WITH ATOMISTIC DETAIL Anna Mapp, Charles Brooks III Nicolas Fawzi (1) (1) University of Michigan (Ann Arbor, United States) (1) Brown University (Providence, United States) POS169 POS176 EXPLORING THE DYNAMICS OF EXBD WITHIN THE TONB SYSTEM OF ESCHE- PHASE SEPARATION OF THE RNA-BINDING PROTEIN FUS IS COOPERATIVELY RICHIA COLI MEDIATED BY AN SYGQ-RICH SEQUENCE AND RGG MOTIFS Dale Kopp (1), Kathleen Postle Anastasia Murthy (1), Nicolas Fawzi (1) The Pennsylvania State University (University Park, United States) (1) Brown University (Providence, United States) POS170 POS177 THE IMPORTANCE OF PROTEIN STRUCTURAL DYNAMICS IN THE ALLOSTERIC HIGH PRESSURE UV-VIS ABSORBANCE SPECTROSCOPY AND ENZYME KINETICS: MECHANISM OF YEAST CHORISMATE MUTASE EFFECTS OF HIGH PRESSURE AND TEMPERATURE ON PROTEASE ACTIVITY Scott Gorman (1), Debashish Sahu, David Boehr Gary Smejkal (1), Vera Gross, Nicole Cutri, Alexander Lazarev (1) The Pennsylvania State University (University Park, United States) (1) Pressure Biosciences (South Easton, United States) POS171 POS178 ENGINEERING THE FIDELITY OF THE VIRAL RNA-DEPENDENT RNA POLYMERASE IN VITRO ANALYSIS OF YBX1 AS A GRANULE-ASSOCIATED INTRINSICALLY BY MODIFYING THE STRUCTURAL DYNAMICS OF THE MOTIF D ACTIVE SITE LOOP DISORDERED PROTEIN Jingjing Shi (1), Jacob Perryman, Xiaorong Yang, Xinran Liu, Jamie Arnold, Mark Liang (1), Anastasia Murthy, Liam O'Connell, Kimberly Mowry, Nicolas Craig Cameron, David Boehr Fawzi (1) Penn State University (University Park, United States) (1) Brown University (Providence, United States) POS172 POS179 NOVEL ATP-CONE-DRIVEN ALLOSTERIC REGULATION OF RIBONUCLEOTIDE HNRNPA2 DISEASE MUTATIONS AND POSTTRANSLATIONAL MODIFICATIONS REDUCTASE VIA THE RADICAL-GENERATING SUBUNIT ALTER LLPS AND PROTEIN-PROTEIN INTERACTIONS Matthew McGann (1), Inna Grinberg, Daniel Lundin, Mikael Crona, Mah- Veronica Ryan (1), Anne Hart, Nicolas Fawzi mudal Hasan, Venkateswara Roa Jonna, Christoph Loderer, Margareta (1) Brown University (Providence, United States) Sahlin, Natalia Markova, John Stenson, Ilya Borovok, Anders Hofer, Derek Logan, Britt-Marie Sjöberg POS180 (1) Malvern Panalytical (Westborough, United States) THE EVOLUTION OF DIVERSE FUNCTIONS WITHIN THE FUNGAL FLAVIN- DEPENDENT HYDROXYLASE FAMILY POS173 Troy Wymore (1), Sara Tweedy, Attabey Rodriguez Benitez, Alison Narayan, HIDDEN DYNAMICS IN THE MECHANICAL UNFOLDING AND REFOLDING OF Charles Brooks III BACTERIORHODOPSIN PROBED WITH 1-ΜS RESOLUTION (1) University of Michigan (Ann Arbor, United States) Thomas Perkins (1), Hao Yu, Mathew Siewny, Devin Edwards (1) NIST & University of Colorado (Boulder, United States) 110 111 #PS32 POS188 MUTATIONAL SCANNING OF Α-SYNUCLEIN IN YEAST REVEALS CRITICAL Posters DETERMINANTS OF TOXICITY Robert Newberry (1), Eric Chow, William DeGrado, Martin Kampmann POS181 (1) University of California, San Francisco (Burlingame, United States) NUCLEAR IMPORT RECEPTOR INHIBITS PHASE SEPARATION OF FUS THROUGH BINDING TO MULTIPLE SITES POS189 Yuh Min Chook (1), Michael Rosen, Takuya Yoshizawa, Rustam Ali, Jenny THE INITIATION OF UBIQUITIN-INDEPENDENT MITOPHAGY BY ATG32 Jio, Ho Yee Joyce Fung, Kathleen Burke, Seung Joong Kim, Yuan Lin, Wil- Michael Ragusa (1), Xue Xia, Sarah Katzenell, Erin Reinhart, Katherine liam Peeples, Daniel Saltzberg, Michael Soniat, Jordan Baumhardt, Rudolf Bauer, Maria Pellegrini Oldenbourg, Andrej Sali, Nicolas Fawzi (1) Dartmouth College (Hanover, United States) (1) University of Texas Southwestern Medical Center (Dallas, United States) POS190 POS183 PROBING CASPASE-NANOGEL SELF-ASSEMBLY AND RELEASE HOW PHOSPHORYLATION PATTERNS OF TAU-441 MODULATE ITS AGGREGA- Francesca Anson (1), Jeanne Hardy, Sankaran Thayumanavan TION PROPENSITY? (1) University of Massachusetts, Amherst (Amherst, United States) Iva Ziu (1) (1) Oakland University (Rochester, United States) POS192 MACROMOLECULAR CROWDING EFFECTS ON BIOMOLECULAR BINDING POS184 FREE ENERGIES: TRENDS OBTAINED THROUGH THEORETICAL “TOY” MODELS RIBOSOME TRANSLOCATION AND FRAMSESHIFTING REVEALED BY A NOVEL Rachel Kim (1), Mala Radhakrishnan FORCE SPECTROSCOPY (1) Wellesley College (Wellesley, United States) Yuhong Wang (1), Heng Yin, Shoujun Xu (1) University of Houston (Houston, United States) POS193 GUIDING THE IMMUNE RESPONSE TO MSP2, AN INTRINSICALLY DISORDERED POS185 MALARIA VACCINE CANDIDATE INVESTIGATING POST-TRANSLATIONAL PROTEIN MODIFICATION MEDIATED Jeffrey Seow (1), Christopher MacRaild, Sreedam Das, Rodrigo Morales, BY DOPAMINE OXIDATION Vashti Irani, Krishnarjuna Bankala, Mitchell Silk, David Chalmers, Jack Rich- Dennis Özcelik (1), Dominik Essig (1) ards, Robin Anders, Raymond Norton (1) University of Copenhagen ( Copenhagen 2100 Denmark, Denmark) (1) Monash (Melbourne, Australia)

POS186 POS194 DIMER INTERFACE MODULATES PROTEIN FOLDING PATHWAYS, COOPERATIV- UNFOLDING MECHANISM OF HGST M1A-1A ITY, AND MISFOLDING IN SINGLE MOLECULES OF SOD1 Kimberley Wiid (1), Stoyan Stoychev, Previn Naicker, Heinrich Dirr Michael Woodside (1), Supratik Sen Mojumdar, Zackary Scholl, Michelle (1) Protein Structure–Function Research Unit, School of Molecular and Sullivan, Craig Garen Cell Biology, University of the Witwatersrand, Johannesburg, South Africa (1) University of Alberta (Edmonton, Canada) (Johannesburg, South Africa)

POS187 POS195 INVESTIGATING THE STRUCTURAL CONFORMATIONS OF ELONGATION FACTOR G STRUCTURALLY-DIRECTED PYRROLYSINE-INSPIRED CYCLIZATION OF THERA- AND THE ROLE OF GTP HYDROLYSIS DURING TRANSLOCATION PEUTIC PROTEINS Zeinab Moussa (1) Marianne Lee (1), Michael K Chan, Lin Wang (1) Self (HOUSTON, United States) (1) The Chinese University of Hong Kong (Shatin, China)

112 113 POS202 #PS32 BINDING OF THE N2A REGION OF TITIN TO F-ACTIN Posters Christopher Tsiros (1), Humra Athar, Matthew Gage (1) UMass Lowell (Dracut , United States) POS196 STRUCTURAL INSIGHT INTO THE METAL-IONS MODULATED CATALYTIC FUNCTION POS203 OF THE BIMETALLIC ENZYME H. PYLORI ARGINASE REPEAT VARIATION AS A SOURCE FOR GENETIC DIVERSITY IN INTRINSICALLY Ankita Dutta (1), Mohit Mazumder, Mashkoor Alam, Samudrala Gourinath, DISORDERED REGIONS IN SACCHAROMYCES CEREVISIAE Apurba Kumar Sau Stephen Fuchs (1), Michael Babokhov, Bradley Reinfeld, Kevin Hackbarth, (1) PhD student (New Delhi, India) Yotam Bentov (1) Tufts University (Medford, United States) POS197 ANTIRETROVIRAL DRUG SUSCEPTIBILITY OF A HINGE REGION VARIANT OF POS204 HIV-1 SUBTYPE C PROTEASE A GENERAL BIOSENSOR STRATEGY FOR E. COLI BASED ON LIGAND-DEPEN- Jake Zondagh (1), Yasien Sayed, Ikechukwu Achilonu, Adriaan Basson, DENT STABILIZATION Vijayakumar Balakrishnan Benjamin Brandsen (1), Jordan Mattheisen, Teia Noel, Stanley Fields (1) University of the Witwatersrand (Johannesburg, South Africa) (1) University of Washington (Seattle, United States)

POS198 POS205 A CONSERVED DISORDER-TO-ORDER TRANSITION IN CCCH ZINC FINGER DISTILLATION OF PROTEIN STABILITY AND EVOLUTIONARY INFORMATION PROTEINS IS REQUIRED FOR EMBRYONIC CYTOKINESIS FROM MULTIPLE SEQUENCE ALIGNMENTS USING A MACHINE LEARNING Francesca Massi (1), Davide Tavella, Katianna Antkowiak, Reyyan Bulut, VARIATIONAL AUTO-ENCODER Sean Ryder Xinqiang Ding (1), Charles Brooks III (1) University of Massachusetts Medical School (Worcester , United States) (1) University of Michigan (Ann Arbor, United States)

POS199 POS206 MECHANISMS OF GENOMIC INSTABILITY IN A REPETITIVE CODING REGION PROBING THE ROLE OF THE EPA1P TANDEM REPEAT REGION IN CANDIDA IN S. CEREVISIAE GLABRATA ADHESION Taylor Stewart (1), Mackenzie Parmenter, Stephen Fuchs Colin Raposo (1), Kyle McElroy, Jessica Ziccarello, Stephen Fuchs (1) Tufts University (Medford, United States) (1) Tufts University (Medford, United States)

POS200 POS207 DEVELOPING AN IGA BIOBETTER ANTIBODY AGAINST E. COLI O157:H7 WITH MICROTUBULE POLYMERIZATION IN THE PRESENCE OF HYPERPHOSPHORY- ENHANCED STABILITY BY RATIONAL DESIGN OF A BOVINE FC CHAIN LATED TAU441 FORMS Adam Chin-Fatt (1), Rima Menassa Saba Anwar (1), Iva Ziu, Sanela Martic (1) Agriculture and Agri-food Canada (London, Canada) (1) Oakland University (Rochester, United States)

POS201 POS208 INVESTIGATION OF TITIN EXPRESSION VARIATION IN MUSCULAR DYSTROPHY REGULATION OF MORPHEEIN BEHAVIOR IN BURKHOLDERIA CENOCEPACIA WITH MYOSITIS SKELETAL MUSCLE TISSUES HMG-COA REDUCTASE Pabodha Hettige (1), Uzma Tahir, Kiisa Nishikawa, Maththew Gage Jeff Watson (1), Chad Hicks, Jean-Claude Abboud (1) Department of Chemistry, University of Massachusetts Lowell (Lowell, (1) Gonzaga University (Spokane, United States) United States)

114 115 POS215 #PS32 LYSINE ACETYLATION AFFECTS LIQUID-LIQUID PHASE SEPARATION AND AM- Posters YLOID FIBRIL FORMATION OF TAU Zhiyang Yao (1), Meng Gao, Zhengding Su, Yongqi Huang POS209 (1) Hubei University of Technology (Wuhan, China) ADP-DEPENDENT KINASES FROM THE ARCHAEAL ORDER METHANOSARCINALES ADAPT TO SALT BY A NON-CANONICAL EVOLUTIONARY CONSERVED STRATEGY POS216 Victoria Guixe (1), Felipe Gonzalez-Ordenes, Pablo Cea, Nicolas Fuentes, INFLUENCE OF STRUCTURE DISORDER ON THE INTERACTION BETWEEN E3 Sebastian Muñoz, Ricardo Zamora, Diego Leonardo, Richard C Garratt, RRNASE AND IM3 Victor Castro-Fernandez, Victoria Guixe Ziting Zhao (1), Meng Gao, Zhengding Su, Yongqi Huang (1) Facultad de Ciencias, Universidad de Chile (Santiago, Chile) (1) Hubei University of Technology (Wuhan, China)

POS210 POS217 ON THE ROLE OF SER/THR KINASE IN PHOSPHORYLATION OF ANABAENA MECHANISM OF DUAL-MOTIF DISORDERED TRANSACTIVATION DOMAIN OF SENSORY RHODOPSIN TRANSDUCER OF ANABAENA PCC 7120 FOXO3A BINDING WITH KIX DOMAIN Aakriti Gautam (1), Vishwa Trivedi Junwen Xiong (1), Meng Gao, Zhengding Su, Yongqi Huang (1) Bethune Cookman University (Daytona Beach, United States) (1) Hubei University of Technology (Wuhan, China)

POS211 POS218 ANALYSIS OF CAMKII ACTIVITY AMONG SPLICE VARIANTS THE INFLUENCE OF FOLDING MECHANISM ON THE COUPLED FOLDING-BIND- Noelle Dziedzic (1), Jack Weeks, Roman Sloutsky, Margaret Stratton ING PROCESS OF INTRINSICALLY DISORDERED PROTEINS (1) University of Massachusetts Amherst (Amherst, United States) Meng Gao (1), Zhengding Su, Yongqi Huang (1) Hubei University of Technology (Wuhan, China) POS212 LIGAND BINDING AND MODULATION OF RECEPTOR BINDING VIA HELICAL POS219 FACE OF ANABAENA SENSORY RHODOPSIN TRANSDUCER, ASRT CONFORMATIONAL TRANSITION OF PROTEIN THROUGH MULTIPLE PATH- Vishwa Trivedi (1), Aakriti Gautam), Tashmay Jones) WAYS: INSIGHT FROM ADENYLATE KINASE (1) Bethune Cookman University (Daytona Beach, United States) Hao Dong (1) (1) Nanjing University (Nanjing, China) POS213 POSSIBLE FUNCTIONAL ROLES FOR PROTEOLYTIC PRODUCTS OF PROTEIN POS220 HORMONES MASSIVELY PARALLEL PROTEIN DESIGN TO DEVELOP ENZYMES FOR Brian Hall (1), Mohamed Anwar, Dennis Cheng, James Hoang, Nurit NEXT-GENERATION CHEMOTHERAPY Haspel, Kenneth Campbell Brahm Yachnin (1), Victor Tan, Laura Azouz, Justin Drake, Sagar Khare (1) Dept. of Biology (Boston, United States) (1) Rutgers University, Department of Chemistry & Chemical Biology (Pisca- taway, United States) POS214 EVOLUTION OF ENVIRONMENTALLY-ENFORCED, REPEAT PROTEIN TOPOLOGY POS221 IN THE OUTER MEMBRANE A GENETICALLY-ENCODED IMMOBILIZED CATALYST FOR BIODIESEL PRODUCTION Joanna Slusky (1), Meghan Franklin, Sergey Nepomnyachiy, Ryan Feehan, Michael Chan (1), Bradley Heater, Marianne Lee Nir Ben-Tal, Rachel Kolodny (1) The Chinese University of Hong Kong (Shatin, China) (1) University of Kansas (Lawrence, United States)

116 117 #PS32 POS229 INTRINSICALLY DISORDERED PROTEINS IN CANCER Posters Zsuzsanna Dosztanyi (1), Balint Meszaros, Andras Zeke, Attila Remenyi POS222 (1) MTA-ELTE Momentum Bioinformatics Group (Budapest, Hungary) DESIGN OF MODULAR SWITCHES FOR ALLOSTERIC CONTROL OVER PROTEIN KINASES AND PROTEIN PHOSPHATASES POS230 Matthew Bienick (1) DEVELOPMENT OF A PH-DEPENDENT NMR CHEMICAL SHIFT PREDICTOR (1) University of Arizona (Tucson, United States) Efrosini Artikis (1), Charles L. Brooks III (1) Biophysics Program (Ann Arbor, United States) POS223 SPIDER SILK: BIOMIMETIC FIBER SELF-ASSEMBLY USING RECOMBINANT POS231 MASP2 SPIDROIN A STRUCTURAL MECHANISM FOR DIRECTING INVERSE AGONISM OF PPARΓ Ali Andres Malay (1), Keiji Numata Douglas Kojetin (1), Richard Brust, Jinsai Shang, Jakob Fuhrmann, Jared (1) RIKEN (Wako-shi, Japan) Bass, Andrew Cano, Zahra Heidari, Ian Chrisman, Anne-Laure Blayo, Pat- rick Griffi n, Theodore Kamenecka, Travis Hughes POS224 (1) The Scripps Research Institute (Jupiter, United States) EVALUATING THE CONTRIBUTION OF HYDROGEN BONDS TO COLLAGEN STABILITY BY CATION-Π INTERACTION INDUCED AAB-TYPE HETEROTRIMERS POS232 Chu-Harn Chiang (1), Yi-Hsuan Fu ENERGY BALANCE AND BISTABILITY IN HISTIDINE KINASE SIGNALING (1) National Tsing-Hua University (Yilan, Taiwan) Bruk Mensa (1), Kathleen Molnar, Andrew Natale, Nicolas Polizzi, William DeGrado POS225 (1) Department of Pharmaceutical Chemistry, UCSF (San Francisco, United CRITICAL BEHAVIORS OF STRUCTURAL FLUCTUATIONS IN THE NATIVE STATES States) OF PROTEINS Wei Wang (1) POS233 (1) Nanjing University (Nanjing, China) MELANOMA-DERIVED HUMAN POLYMERASE THETA VARIANTS EXHIBIT AL- TERED DNA POLYMERASE ACTIVITY POS226 Jorge Victorino (1), Lisbeth Avalos, Greg Rebelo LOOP STRUCTURES OF OUTER MEMBRANE BETA-BARRELS (1) Rhode Island College (Providence, United States) Meghan Franklin (1), Joanna Slusky (1) University of Kansas (Lawrence, United States) POS234 PROTABANK: A REPOSITORY FOR PROTEIN DESIGN AND ENGINEERING DATA POS227 Connie Wang (1), Paul Chang, Marie Ary, Stephen Mayo, Barry Olafson IDENTIFICATION POTENTIAL DRUG TARGETS IN LEISHMANIA DONOVANI (1) Protabit LLC (Pasadena, United States) USING PROTEIN-PROTEIN INTERACTION NETWORK (PPIN) ANALYSIS AND MOLECULAR DYNAMICS KNOCK-OUT STUDIES POS235 Kalyani Dhusia (1), Ranjit Maurya, Pramod Yadav SITE-SPECIFIC LABELING OF DNA POLYMERASE THETA WITH 5-FAM CADAVERINE (1) Sam Higginbottom University of Agriculture, Technology and Sciences Ashley Rebelo (1), Jorge Victorino (Allahabad, India) (1) Rhode Island College (Providence, United States)

POS228 POS236 THE STRUCTURAL BASIS FOR CARD9 AND CARD11 AUTOINHIBITION MOLECULAR DETERMINANTS OF INTRACELLULAR TRAFFICKING IN TETANUS Michael Holliday (1), Axel Witt, Alberto Estevez, Alexis Rohou, Erin Dueber, NEUROTOXIN Wayne Fairbrother Sulyman Barkho (1), Jie Zhang, Liang Tao, Min Dong (1) Genentech (South San Francisco, United States) (1) Boston Children's Hospital (Boston, United States) 118 119 POS243 #PS32 HIGH-RESOLUTION STRUCTURE OF CLPC1-NTD-RUFOMYCIN COMPLEX PRO- Posters VIDES THREE-DIMENSIONAL FRAMEWORK FOR OPTIMIZATION OF CYCLOPEP- TIDE ANTI-TB DRUG LEADS POS237 Nina Wolf (1), Hyun Lee, Mary Choules, Larry Klein, Valentina Petukhova, THE IMPORTANCE OF TYROSINE OVER TRYPTOPHAN IN BINDING TRIMETHYL- Michael Tufano, Rasika Phansalkar, Wei Gao, Bernard Santarsiero, Hanki LYSINE IN THE AROMATIC CAGE OF THE HP1 CHROMODOMAIN Lee, Ying-Yu Jin, Ngoc Anh Ho, Celerino Abad-Zapatero, Guido Pauli, Katherine Albanese (1), Mackenzie Krone, Alex Guseman, Gary Pielak, Scott Franzblau, Sanghyun Cho Marcey Waters, Eric Brustad (1) University of Illinois at Chicago (Chicago, United States) (1) University of North Carolina at Chapel Hill (Chapel Hill, United States) POS244 POS238 ON-CHIP MEASUREMENTS OF MEMBRANE PROTEIN INTERACTIONS STIMULUS-RESPONSIVE SELF-ASSEMBLY OF ENZYMATIC FRACTALS BY Yuewen Zhang (1), Tuomas Knowles, Sara Linse COMPUTATIONAL DESIGN (1) University of Cambridge (Cambridge, United Kingdom) Nancy Hernandez (1),William Hansen, Denzel Zhu, Maria Shea, Marium Khalid, Viacheslav Manichev, Matthew Putnins, Muyuan Chen, Anthony POS245 Chen, Lu Yang, Melissa Banal, Sang-Hyuk Lee, Lawrence Wackett, Wei NATIVE HYPERSTABLE PROTEIN EXPRESSION IN BACTERIAL PATHOGENS Dai, Sagar Khare Jane Thibeault (1), Blanca Barquera, Wilfredo Colon (1) Rugers University (East Brunswick, United States) (1) Rensselaer POlytechnic Institute (Troy, United States) POS239 POS246 ENZYME ACTIVITY AND SPECIFICITY MODULATED BY PROTEIN FILAMENTATION IDENTIFYING HSP60 INHIBITORS WITH SELECTIVE CYTOTOXICITY TO COL- N Horton (1), Chad Park, Jonathan Sanchez, Claudia Barahona, Emilia ORECTAL CANCER CELLS Basantes Steven Johnson (1), Anne-Marie Ray, Sanofar Abdeen, Nilshad Salim, (1) University of Arizona (Tucson, United States) Andrew Ambrose, Yagnshin Park, Quyen Hoang, Eli Chapman, Steven Johnson POS240 (1) Indiana University School of Medicine (Indianapolis, United States) EXPLORING THE BASIS FOR SUBSTRATE DISCRIMINATION IN FLAVIN-DEPEN- DENT HYDROXYLASE CATALYSIS WITH A COMBINED QM/MM APPROACH POS247 Sara Tweedy (1), Attabey Rodríguez Benítez, Alison R.H. Narayan, Charles EXPRESSION OF TAU IN SACCHAROMYCES CEREVISIAE TO DETERMINE THE L. Brooks III, Troy Wymore EFFECTS OF N-TERMINAL ACETYLATION (1) University of Michigan (Ann Arbor, United States) Jess Anderson (1), William Holmes (1) Rhode Island College (Providence, United States) POS241 STRUCTURE-GUIDED MUTAGENESIS OF DNA RECOGNITION MOTIFS IN APOBEC3A POS248 Samantha Ziegler (1), Yong Xiong COMPUTATIONAL DESIGN OF A PHOTOSENSITIZED YEAST CYTOSINE DEAMI- (1) Yale University (New Haven, United States) NASE FOR DIRECTED ENZYME-PRODRUG THERAPY Kristin Blacklock (1), Brahm Yachnin, G. Andrew Woolley, Sagar Khare POS242 (1) Rutgers, The State University of NJ (Piscataway, United States) CONSERVED SALT-BRIDGE COMPETITION TRIGGERED BY PHOSPHORYLATION REGULATES THE PROTEIN INTERACTOME POS249 John Skinner (1), Sheng Wang, Jiyoung Lee, Colin Ong, Ruth Sommese, PROTEASOMAL SUBSTRATE PROCESSING REQUIRES CONFORMATIONAL Sivaraj Sivaramakrishnan, Wolfgang Koelmel, Maria Hirschbeck, Hermann SWITCHING BY AN ALLOSTERIC NETWORK IN THE REGULATORY PARTICLE Schindelin, Caroline Kisker), Kristina Lorenz, Tobin Sosnick, Marsha Rosner Eric Greene (1), Ellen Goodall, Andres Hernandez, Mary Matyskiela, Gabriel (1) University of Pennsylvania (Philadelphia, United States) Lander, Andreas Martin 120 (1) University of California at Berkeley (Berkeley, United States) 121 POS257 #PS32 DUBIOUS LIGANDS IN PROTEIN CRYSTAL STRUCTURES MAY LEAD TO NON-RE- Posters PRODUCIBILITY IN STRUCTURE-BASED DRUG DISCOVERY POS250 Ivan Shabalin (1), Wladek Minor INVESTIGATING THE MUTATION TOLERANCE OF THE DIPHTHAMIDE HISTIDINE (1) UNIVERSITY OF VIRGINIA (Charlottesville, United States) IN HUMAN ELONGATION FACTOR 2 John Weldon (1), Benjamin Atha, Jack Sanford, Lauren Russell POS258 (1) Towson University (Towson, United States) ACQUISITION OF A BOTULINUM NEUROTOXIN-LIKE TOXIN BY ENTEROCOC- CUS FAECIUM POS251 Sicai Zhang (1) THE HECT C-TERMINAL LOBE OF HERC6 REVEALS A UNIQUE AUTOINHIBITORY (1) Boston Children's hospital (Boston, United States) DOMAIN SWAPPING MECHANISM Donald Spratt (1), Yaya Wang, Andrew Bellesis, William Royer POS259 (1) Clark University (Worcester, United States) AROMATIC RESIDUES IN THE HEAD DOMAIN OF THE INSECTICIDAL PROTEIN CRY51AA2.834_16 MEDIATE INTERACTION WITH A SPECIFIC PROTEIN RECEP- POS252 TOR IN LYGUS SP., CONFERRING TARGET SPECIFICITY ENGINEERING SUPER READERS FOR CHROMATIN RESEARCH Jeffrey Haas (1), Jean-Louis Kouadio, Yanfei Wang, Pardeep Kumar, Jin- Mackenzie Krone (1), Katherine Alabanese, Marcey Waters, Eric Brustad ling Wang, Timothy Rydel, Jennifer Howard, Brian Weiner, Andrew Henry, (1) UNC-Chapel Hill (Chapel Hill, United States) Agoston Jerga (1) Monsanto (Chesterfi eld, United States) POS253 STRUCTURE AND MECHANISM OF AN EXCEPTIONALLY POWERFUL MOTOR POS260 THAT POWERS VIRUS ASSEMBLY SYNTHETIC GENERATION OF A MULTI-SUBUNIT CHLAMYDIA VACCINE Brian Kelch (1), Janelle Hayes, Nicholas Stone, Brendan Hilbert Wei He (1), Matthew Coleman (1) University of Massachusetts Medical School (Worcester, United States) (1) Lawrence LIvermore National Laborotary (Livermore, United States)

POS254 POS261 GETTING IN THE GROOVE: CHAPERONE-ASSISTED PEPTIDE EXCHANGE DY- NMR-BASED DESIGN OF A HYBRID THERMOPHILIC/MESOPHILIC ENZYME NAMICS IN THE MAJOR HISTOCOMPATIBILITY COMPLEX WITH ENHANCED HIGH-TEMPERATURE ACTIVITY Nikolaos Sgourakis (1), Andrew McShan, Kannan Natarajan, Vlad Kumirov, David Vincenzo Venditti (1), Rochelle Dotas Flores-Solis, Jiansheng Jiang, Jugmohit Toor, Evgenii Kovrigin, David Margulies (1) Iowa State University (Ames, United States) (1) UCSC (Santa Cruz, United States) POS262 POS255 BIOCHEMICAL AND STRUCTURAL STUDIES OF A HIV CA BINDING NANOBODY SOLVING PROTEIN STRUCTURE USING GENETICS Eva Gerber (1), Sarah Smaga, Brady Summers, Katie Digianantonio, Yong Jörn Schmiedel (1), Ben Lehner Xiong (1) Centre for Genomic Regulation (CRG) (Barcelona, Spain) (1) Yale University (New Haven, United States)

POS256 POS263 INVESTIGATING NATIVE-STATE PROTEIN DYNAMICS THROUGH SIMULATIONS UNRAVELING THE EXOCYST COMPLEX: SUBUNIT ACCESSIBILITY REVEALS A OF HYDROGEN EXCHANGE MASS SPECTROMETRY AND BAYESIAN ANALYSIS MECHANISM TO REGULATE SNARE-MEDIATED VESICLE FUSION OF EXPERIMENTAL DATA Dante Lepore (1), Michael Feyder, Chanwoo Lee, Sang-Hyun Rah, Lillian John Strahan (1), Sheila Jaswal Kenner, Tae-Young Yoon, Adam Frost, Mary Munson (1) Amherst College (Sudbury MA, United States) (1) Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School (Worcester, United States) 122 123 POS271 #PS32 A GRAPH THEORETICAL APPROACH FOR DECIPHERING RESIDUE CHARAC- Posters TERISTICS IN ALLOSTERIC COMMUNICATION PATHS POS264 Girik Malik (1), Anirban Banerji, Maksim Kouza, Irina Buhimschi, Andrzej PROTEIN ENGINEERING TO GENERATE PROTEIN-BASED INHIBITORS OF CAN- Kloczkowski CER AND STEM CELL SIGNALING PATHWAYS AND TO ENABLE THE REPRO- (1) Nationwide Children's Hospital (Columbus, United States) DUCIBLE CRYSTALLIZATION OF RECALCITRANT PROTEINS James Moody (1), Martin Lawrence, Lyra Griffi ths, Shiri Levy, Julie Mathieu, POS273 Yalan Xing, Woojin Kim, Brenda Schulman, Richard Kriwacki, Stuart Orkin, POLYMER-ENCAPSULATED NANODISCS GENERATES DISTINCT PATHOLOGICAL Catherine Drennan, Hannele Ruohola-Baker, Michael Dyer, David Baker, PHENOTYPES OF TYPE-II DIABETES AND ALZHEIMER’S AMYLOID INTERMEDIATES Joan Broderick Bikash Sahoo (1), Takuya Genjo, Ayyalusamy Ramamoorthy (1) Brigham Young University (Provo, United States) (1) University of Michigan (Ann Arbor, United States)

POS265 POS274 CA++ STABILIZATION EFFECT ON IMMUNOGLOBULIN DOMAINS IN TITIN’S N2A PH-MEDIATED PROCESSES IN THE INTEGRAL MEMBRANE INFLUENZA A PROTON REGION CHANNEL (AM2) STUDIED BY CONSTANT PH MOLECULAR DYNAMICS Colleen Kelly (1) Hedieh Torabifard (1), Afra Panahi, Charles. L. Brooks III (1) University of Massachsuetts Lowell (Milford, United States) (1) Department of Chemistry, University of Michigan (Northville, United States) POS266 SINGLE-STRANDED TELOMERE BINDING PROTEINS EMPLOY PLASTIC RECOG- POS275 NITION TO TUNE BINDING AFFINITY AND SPECIFICITY THAT DRIVES FUNCTION AN EFFECTIVE ONE-STEP PURIFICATION OF THE HSP70 CHAPERONE SSA1 Deborah Wuttke (1), Thayne Dickey, Neil Lloyd, Sarah Altschuler, Leslie FROM SACCHAROMYCES CEREVISIAE Glustrom, Ken Lyon, Margherita Paschini, Cynthia Reyes, Victoria Lundblad Alijah A. Griffi th (1), William Holmes (1) University of Colorado (Boulder, United States) (1) Rhode Island College (Blackstone, United States)

POS267 POS276 RAPID CHARACTERIZATION OF ADALIMUMAB WITH THE LABCHIP GXII PREDICTION OF PROTEIN AGGREGATION PROPENSITIES WITH SPINE-X TOUCH HT Andrzej Kloczkowski (1), Eshel Faraggi, Maksim Kouza, Girik Malik, Irina April Blodgett (1), Janet Buecker, Brian Gerwe, Laurel Provencher Buhimschi (1) PerkinElmer (Arlington, United States) (1) Nationwide Children's Hospital and The Ohio State University (Colum- bus, United States) POS269 DUAL CHAPERONE FUNCTION IN NASCENT PROTEIN FOLDING POS277 Christian Kaiser (1), Kaixian Liu, Kevin Maciuba MYCOBACTERIAL CLPS BINDS N-END-RULE PEPTIDES AND THE AAA+ UNFOL- (1) Johns Hopkins University (Baltimore, United States) DASE CLPC1 Christopher Presloid (1), Karl Schmitz, Thomas Swayne POS270 (1) University of Delaware (Newark, United States) PROTEOME-WIDE MODULATION OF DEGRADATION DYNAMICS IN RESPONSE TO GROWTH ARREST POS278 Sina Ghaemmaghami (1), Tian Zhang, Kevin Welle DETERMINING THE EFFECTS OF N-TERMINAL ACETYLATION ON MICROTUBULE (1) University of Rochester (Rochester, United States) ASSOCIATED PROTEIN TAU William Holmes (1), Anna Lally (1) Rhode Island College (Providence, United States) 124 125 POS285 #PS32 COUPLING OF THE REDOX AND STRUCTURAL STATES IN CYTOCHROME P450 Posters REDUCTASE STUDIED BY MOLECULAR DYNAMICS SIMULATION POS279 Mikuru Iijima (1), Jun Ohnuki, Takato Sato, Masakazu Sugishima, Mitsunori Takano CA2+-INDEPENDENT CARBOHYDRATE-RECOGNITION OF THE C-TYPE LEC- (1) Department of Pure and Applied Physics, Waseda University (Shin- TINS, SPL-1 AND SPL-2, FROM THE BIVALVE SAXIDOMUS PURPURATUS AND juku-ku, Japan) THEIR DIMERIZATION PROPERTIES Shuhei Higuchi (1), Hideak Unno, Shuichiro Goda, Tomomitsu Hatakeyama POS286 (1) Graduate School of Engineering, Nagasaki University (Nagasaki, Japan) DETERMINING BINDING AFFINITIES OF A NEISSERIA MENINGITIDIS CAPSULE POLYMERASE WITH NUCLEOTIDE DONOR SUBSTRATES POS280 Pumtiwitt McCarthy (1), Abeer Sharyan, Cendy Gonzalez, Ophelia CHARACTERIZING THE CD47/TSP-1 SIGNALING AXIS Ukaegb), Kayla Powell Sarah Young (1), Su Chung, William Montfort (1) Morgan State University (Baltimore, United States) (1) The University of Arizona (Tucson, United States) POS287 POS281 THERMODYNAMIC STABILITY OF POLAR AND NON-POLAR AMYLOID FIBRILS A DESIGNED L-LACTATE DEHYDROGENASE DERIVED FROM L-LACTATE OXIDASE Cristiano Dias (1), Farbod Mahmoudinobar BY OXYGEN ACCESSIBLE PATHWAY ENGINEERING (1) New Jersey Institute of Technology (Newark, United States) Kentaro Hiraka (1), Katsuhiro Kojima, Chi-En Lin, Wakako Tsugawa, Ryutaro Asano, Hiromi Yoshida, Jeffrey La Belle, Koji Sode POS288 (1) Department of Biotechnology and Life Science, Graduate School of PROBING CLASS C G PROTEIN-COUPLED RECEPTOR STRUCTURE AND FUNC- Engineering, Tokyo University of Agriculture and Technology (Koganei, TION VIA OPTICAL SENSING AND MANIPULATION Japan) Jordana Thibado (1), Joshua Levitz (1) Weill Cornell Medicine (New York, United States) POS282 CHARACTERIZATION AND RESCUE OF ENDOCYTIC AND LIPID HOMEOSTATIC POS289 DISRUPTIONS CAUSED BY APOE4 MOLECULAR DYNAMICS PREDICTION OF THE SUBSTRATE-BINDING SITES AND Priyanka Narayan (1), Grzegorz Sienski, Yuan-Ta Lin, Jinsoo Seo, Julia LIGATION MECHANISM IN POLY-Α-GLUTAMATE SYNTHETASE RIMK Bonner, Valeriya Baru, Aftabul Haque, Yelena Freyzon, Nora Kory, Elizave- Jun Ohnuki (1), Yasuhiro Arimura, Tomonori Kono, Kuniki Kino, Hitoshi Kuru- ta Frienkman, Caroline Lewis, Julie Valastyan, Sebastian Boland, David mizaka, Mitsunori Takano Sabatini, Li-Huei Tsai, Susan Lindquist (1) Department of Pure and Applied Physics, Graduate School of Ad- (1) Picower Institute, MIT (Cambridge, United States) vanced Science and Engineering, Waseda University (Shinjuku-Ku, Japan)

POS283 POS290 RELATIONSHIP BETWEEN KINETICS AND MECHANICAL STABILITY OF THE FIBRIL AΒ42 OLIGOMER HETEROGENEITY AS AN ORIGIN FOR AMYLOID FIBRIL POLY- STATE AND FIBRIL FORMATION TIMES OF PEPTIDES: A COMPUTATIONAL STUDY MORPHISM Maksim Kouza (1), Nguyen Truong Co, Mai Suan Li, Sebastian Kmiecik, Zhefeng Guo (1), Christine Xue, Joyce Tran, Hongsu Wang, Frederick Hsu Andrzej Kolinski, Andrzej Kloczkowski, Irina Buhimschi (1) University of California, Los Angeles (Los Angeles, United States) (1) Nationwide Children’s Hospital (Columbus, United States) POS291 POS284 DUAL ROLE OF ZINC FINGERS FOR PROTEIN AND DNA INTERACTIONS IN PROBING THE PYRAZINAMIDE RESISTANCE MECHANISM IN RIBOSOMAL PRO- NUCLEAR IMPORT OF TRANSCRIPTION FACTOR SP1 TEIN S1 (RPSA) MUTANT OF MYCOBACTERIUM TUBERCULOSIS Jun Kuwahara (1), Chisana Uwatoko Aditi Singh (1), Pallavi Somvanshi, Abhinav Grover (1) Doshisha Women's University (Kyotanabe, Japan) (1) TERI School of Advanced Studies (New Delhi, India) 126 127 #PS32 POS302 BIOCHEMICAL CHARACTERIZATION OF MUTANT C9ORF72 DIPEPTIDE REPEAT Posters STRUCTURES, SEQUENCES IMPLICATED IN AMYOTROPHIC LATERAL SCLERO- POS292 SIS, AND THEIR INTERACTIONS WITH G-QUADRUPLEX DNA STRUCTURES APPLICATION OF IN-CELL PROTEIN FOOTPRINTING COUPLED WITH MASS SPEC- Karl Vosatka (1), Ino Chough, Bashkim Kokona, Robert Fairman TROMETRY TO STUDY PROTEIN STRUCTURE DIRECTLY IN THE NATIVE CELLULAR (1) Haverford College (Haverford, United States) ENVIRONMENT Lisa Jones (1), Dante Johnson, Emily Chea, Upneet Kaur, Jessica Espino POS303 (1) University of Maryland (Baltimore, United States) HSP104 CAN DISSAGREGATE INCLUSION BODIES IN DROSOPHILA MELANO- GASTER, FORMED BY THE POLYGA DIPEPTIDE REPEAT MUTANT PROTEIN FORM POS295 OF C9ORF72, A PROTEIN KNOWN TO BE INVOLVED AMYOTROPHIC LATERAL THE ROLE OF CAMKII ALTERNATIVE SPLICING IN LONG-TERM MEMORY FORMATION SCLEROSIS Roman Sloutsky (1), Christine Battle, Margaret Stratton Emma Robinson (1), Zoe Wong, Sophia Nelson, Bashkim Kokona, Robert (1) University of Massachusetts Amherst (Sunderland, United States) Fairman (1) Haverford College (Haverford, United States) POS296 MINC N- AND C-DOMAIN INTERACTIONS REGULATE ESCHERICHIA COLI FTSZ POS304 ASSEMBLY, DIVISION SITE SELECTION, AND MIND-DEPENDENT OSCILLATION HETEROLOGOUSLY EXPRESSED GEOBACTER SULFURREDUCENS PILA PROTEIN Chris LaBreck (1), Joe Conti, Marissa Viola, Jodi Camberg CAN BE PURIFIED AND RECONSTITUTED TO FORM ELECTRONICALLY ACTIVE (1) University of Rhode Island (north kingstown, United States) FIBRILS SIMILAR TO THEIR NATIVE PROPERTIES IN THIS ANAEROBIC BACTERIUM Jillian Wu (1), Helen Jung, Bashkim Kokona, Robert Fairman POS297 (1) Haverford College (Haverford, United States) ANALYSIS OF PROTEIN SEQUENCE AND STRUCTURAL CONSEQUENCES OF AMI- NO ACID VARIANTS ASSOCIATED WITH AUTOIMMUNE INFLAMMATORY BOWEL POS305 DISEASE DETERMINATION OF BAG-1 AND HEAT SHOCK PROTEINS INTERACTION NET- Constance Jeffery (1), Chang Chen WORKS IN BREAST CANCER CELL LINES (1) University of Illinois at Chicago (Chicago, United States) Tugba Kizilboga Akgun (1), Nisan Denizce Can, Baran Dingiloglu, Ezgi Bas- turk, Can Ozden, Evren Onay Ucar, Gizem Dinler Doganay POS298 (1) Istanbul Technical University (Istanbul, Turkey) A SYNTHETIC MOLECULAR CAGE ENABLES PROTEIN REFOLDING Daishi Fujita (1), Ryoto Suzuki, Makoto Fujita POS307 (1) Kyoto University (Kyoto, Japan) THE ALLOSTERIC MECHANISMS DRIVING THE EVOLUTION OF ANDROGEN SPECIFICITY POS300 Denise Okafor (1), Jennifer Colucci, Eric Ortlund DEVELOPING A ROBUST REPORTER SYSTEM TO EVALUATE AND IMPROVE (1) Emory University (Atlanta, United States) AMBER SUPPRESSION IN YEAST Jessica Stieglitz (1), Haixing Kehoe, James Van Deventer POS308 (1) Department of Chemical and Biological Engineering, Tufts University E. COLI ADENYLATE KINASE EXHIBITS COUPLING BETWEEN LID AND CORE (Medford, United States) DOMAINS Joseph Rehfus (1), Vincent Hilser POS301 (1) Johns Hopkins University (Baltimore, United States) EXAMINING THE EFFECT OF UBIQUITINATION ON THE ENERGY LANDSCAPES OF SUBSTRATE PROTEINS Emma Carroll (1), Andreas Martin, Susan Marqusee (1) UC Berkeley (Berkeley, United States) 128 129 POS315 #PS32 ANTI-APOPTOTIC BAG-1S ISOFORM IS INVOLVED IN ENDOPLASMIC RETICU- Posters LUM ASSOCIATED DEGRADATION Nisan Denizce Can (1), Tuğba Kızılboğa Akgün, Baran Dingiloğlu, Serena POS309 Muratçıoğlu, Efe Elbeyli, Özlem Keskin, Gizem Dinler Doğanay CHEMO-MECHANICAL COUPLING MECHANISM OF ROTATION OF MAMMALI- (1) Istanbul Technical University (Istanbul, Turkey) AN F1-ATPASE BY STATIC AND DYNAMIC X-RAY CRYSTALLOGRAPHIC STUDIES Toshiharu Suzuki (1), Kunio Hirata, Eiki Yamashita, Seiki Baba, Naoya Iida, POS316 Takashi Kumasaka, Toshiya Endo, Toru Hisabori, Masasuke Yoshida, Hiroyuki MECHANISTIC INSIGHT INTO PKC REGULATORY REGION INTERACTIONS WITH Noji ANIONIC MEMBRANES (1) Dept of Applied Chem, School of Eng, The University of Tokyo (Tokyo, Taylor Cole (1), Dhanusree Viswanathan, Tatyana Igumenova Japan) (1) Texas A&M University (College Station, United States)

POS310 POS317 STRUCTURAL DYNAMICS OF THE DNA-BINDING DOMAIN OF HUMAN FOXP1 BAG-1 ISOFORMS INTERACT DIFFERENTIALLY WITH CELL SURVIVAL PATHWAY IN THE DISSOCIATION PATHWAY AND PROTEIN HOMEOSTASIS REGULATORS TO MODULATE CANCER PRO- Jorge Babul (1), Exequiel Medina, Hugo Sanabria, César A. GRESSION IN BREAST CANCER CELLS Ramírez-Sarmiento Gizem Dinler Doganay (1), Nisan Denizce Can, Tugba Kizilboga, Sevilay (1) Universidad de Chile (Santiago, Chile) Acar, Serena Muratcıoglu, Efe Elibeyli, Ozlem Keskin (1) Istanbul Technical University (Istanbul, Turkey) POS311 MOLECULAR MECHANISM UNDERLYING THE HIJACKING OF HOST PROTEINS POS318 BY NONSTRUCTURAL PROTEIN 1 OF 1918 INFLUENZA A VIRUS COSOLUTE EFFECTS ON A DOMAIN-SWAPPED HOMODIMER Qingliang Shen (1), Danyun Zeng, Jae-Hyun Cho Gerardo Perez Goncalves (1), Alex Guseman, Shannon Speer, Gary Pielak (1) Texas A&M University (College Station, United States) (1) Department of Chemistry, University of North Carolina at Chapel Hill (Chapel Hill, United States) POS312 THE ROLE OF THE FURIN-CLEAVABLE LINKER AND KDEL SEQUENCE IN CYTO- POS320 TOXICITY OF RECOMBINANT IMMUNODNASE CAN GLYCOSYLATION STABILIZE THE PREFUSION CONFORMATION OF HCMV Jillian Baker (1), John Weldon FUSOGENIC GLYCOPROTEIN B? (1) Towson University (Baltimore, United States) Ellen White (1), Katya Heldwein (1) Tufts University (Boston, United States) POS313 NMR CHARACTERIZATION OF CHANGES IN ACID-STRESS BACTERIAL CHAP- POS321 ERONE HDEA AS A FUNCTION OF PH IN PREPARATION FOR ACTIVATION MOLECULAR MODULATORS OF UBQLN2 AGGREGATION: IMPLICATIONS IN Karin Crowhurst (1), Marlyn Widjaja, Jafaeth Gomez AGING AND NEURODEGENERATION (1) California State University Northridge (Northridge, United States) Magdalena Ivanova (1), Lisa Sharkey, Nathaniel Safren, Amit Pithadia, Julia Gerson, Mark Dulchavsky, Molly Soper, John Kim, Alia Meliki, Ronak POS314 Patel, Naila Ashraf, Gabrielle Lantis, Eiko Minakawa, Brandon Ruotolo, STRUCTURAL ANALYSIS OF LIMONENE SYNTHASE COMPLEXED WITH A SUB- Sami Barmada, Henry Paulson STRATE ANALOG MIMICKING THE PRE-CYCLIZATION REACTION INTERMEDIATE (1) Department of Neurology and Biophysics Program, University of Michi- Prem Ramasamy (1), Benjamin Morehouse, Qi Yu, Daniel Oprian gan, and Protein Folding Disease Initiative, University of Michigan Medical (1) Brandeis University (Waltham, United States) School (Ann Arbor, United States) 130 131 POS329 #PS32 STRUCTURAL BIOLOGY IN CELLULAR ENVIRONMENTS USING HIGH SENSITIVITY NMR Posters Kendra Frederick (1) POS322 (1) UT Southwestern (Dallas, United States) STRUCTURE OF THE HUMAN TRPM4 ION CHANNEL IN A LIPID NANODISC Henriette Autzen (1), Alexander Myasinikov, Melody B. Campbell, Daniel POS330 Asarnow, David Julius, Yifan Cheng IN SILICO RESIDUE SCANNING TO IDENTIFY KEY ELECTROSTATIC INTERACTIONS (1) UCSF (San Francisco, United States) FOR PROTEIN ENGINEERING Timothy Coulther (1), Penny Beuning, Mary Jo Ondrechen POS323 (1) Northeastern University (Allston, United States) DISCOVERY AND CHARACTERIZATION OF BACTERIAL POLYMORPHIC TOXIN SYSTEMS POS331 Dapeng Zhang (1), Lakshminarayan Iyer, Max Burroughs, Jun Zheng, L INCORPORATING HIERARCHICAL KINETICS INTO DETERMINATION OF PROTEIN Aravind STRUCTURE (1) Saint Louis University (Clayton, United States) Colin Smith (1), Adam Mazur, Ashok Rout, Christian Griesinger, Donghan Lee, Bert de Groot POS324 (1) Wesleyan University (Middletown, United States) NOVEL PROBES FOR STUDYING OXIDATIVE STRESS IN VIVO Oshini Ekanayake (1), Samuel Scinto, Joseph Fox, Sharon Rozovsky POS332 (1) University of Delaware (Newark, United States) FIRST RESULTS FROM LCLS X-RAY DIFFRACTION STUDIES OF CRYSTALLINE APOA1 NANODISCS POS325 Megan Shelby (1), Deepshika Gilbile, Tom Grant, Carolin Seuring, Wei He, ENGINEERING AN ADAPTABLE MECHANISM FOR BIOSENSOR DEVELOPMENT Angela Evans, Tim Pakendorf, Pontus Fischer, Alex Batyuk, Mark Hunter, Maria Presti (1), Stewart Loh, Jeung-Hoi Ha Miriam Barthelmess, Alke Meents, Matthias Frank, Matt Coleman (1) SUNY Upstate Medical University, Dept. of Biochemistry and Molecular (1) Lawrence Livermore Lational Lab (Livermore, United States) Biology (Syracuse, United States) POS333 POS326 IMPORTANCE OF ELECTROSTATIC INTERACTIONS IN NATURAL ENZYMES: WHEN REDESIGN TAKES YOU TO STRANGE PLACES: THE CASE OF L117K MU- WHAT CAN WE LEARN FOR PROTEIN ENGINEERING? TANT OF THE LYSINE ARGININE BINDING PROTEIN Mary Jo Ondrechen (1), Timothy A. Coulther, Lisa Ngu, Penny J. Beuning Diego Granados (1), Jesus Banda-Vazquez, Alejandro Sosa-Peinado (1) Northeastern University (Boston, United States) (1) Biochemistry Department, School of Medicine, UNAM, Mexico (Mexico City, Mexico) POS334 COMPUTATIONAL STUDIES OF THE ROLE OF DISTAL RESIDUES IN HUMAN POS327 PHOSPHOGLUCOSE ISOMERASE CATALYSIS A NOVEL SCAFFOLD OF MDM2/MDMX DUAL INHIBITOR Shanadeen C. Begay (1), Penny J. Beuning, Mary Jo Ondrechen Xiyao Cheng (1), Rong Chen, Changzheng Cao, Ziting Zhao, Meng Cao, (1) Northeastern University (Boston, United States) Yongqi Huang, Huili Liu, Zhengding Su (1) Hubei University of Technology (Wuhan, China) POS335 THE DESIGN RULES OF SELF-ASSEMBLED COLLAGEN MIMETIC PROTEIN FIBRILS POS328 WITH AXIAL REPEATING D-PERIOD THE ROLE OF FLEXIBLE REGIONS IN PROTEIN KINASE C REGULATION Yujia Xu (1), Fang Fang Chen, Parminder Jeet Kaven, Faizunnahar Dewan, Tatyana Igumenova (1), Yuan Yang, Taylor Cole, Dhanusree Viswanathan Carl Guenst, Jui Shivaji Chaugule (1) Texas A&M University (College Station, United States) (1) Department of Chemistry, Hunter College of CUNY (New York, United States) 132 133 #PS32 POS344 STRUCTURE AND FUNCTION OF RNA METHYLTRANSFERASES Posters Yunsun Nam (1) POS336 (1) UT Southwestern Med Ctr (Dallas, United States) HIGH RESOLUTION FUNCTIONAL INTERACTION OF A MINIMAL CYP450-RE- DOX COMPLEX IN LIPID BILAYER POS345 Mukesh Mahajan (1), Elke Prade, Sang-Choul Im, Meng Zhang, Katherine PROBING THE FUNCTIONAL AND DISEASE CONSEQUENCES OF POPULATING Gentry, G.M Anantharamaiah, Lucy Waskell, Ayyalusamy Ramamoorthy AN RNA RECOGNITION MOTIF INTERMEDIATE STATE, A COMMON FEATURE IN (1) University of Michigan (Ann Arbor, United States) A SET OF AMYOTROPHIC LATERAL SCLEROSIS-LINKED RNA-BINDING PROTEINS Jill Zitzewitz (1), Brian C. Mackness, Connor E. Maguire, Elizabeth M. DiLore- POS337 to, Lidette M. Angeles-Perez, Muska Hassan, Kevin O. Boettger, Selma Er- CRYOEM STRUCTURES OF CLPXP COMPLEX AT ATOMIC RESOLUTION endira Avendano-Vazquez, Brittany Morgan, C. Robert Matthews, Osman Xue Fei (1) Bilsel, Francesca Massi, Jill A. Zitzewitz (1) MIT (cambridge, United States) (1) University of Massachusetts Medical School (Worcester, United States)

POS339 POS346 INTERPRETATION OF SOLUTION X-RAY SCATTERING DATA FROM LIPID NANODISCS LEADING ROLE OF TBP IN THE ESTABLISHMENT OF COMPLEXITY IN EUKARY- Lin Yang (1), Vito Graziano, Lisa Miller OTIC TRANSCRIPTION INITIATION SYSTEMS (1) Brookhaven National Laboratory (Upton, United States) Naruhiko Adachi (1), Eiryo Kawakami, Toshiya Senda, Masami Horikoshi (1) SBRC, IMSS, KEK (Tsukuba, Japan POS340 PHOSPHOLIPIDS REGULATE THE INTERACTIONS BETWEEN ESSENTIAL BACTERI- POS347 AL CELL DIVISION PROTEINS FTSA AND FTSZ TO BUD OR NOT TO BUD: INHIBITION OF THE HSV-1 NUCLEAR EGRESS COMPLEX Joseph Conti (1), Evelyn Siler, Jodi L. Camberg Elizabeth Draganova (1), Ekaterina Heldwein (1) University of Rhode Island (kingston, United States) (1) Department of Molecular Biology and Microbiology, Tufts University School of Medicine (Boston, United States) POS341 MULTISITE Λ DYNAMICS PREDICTS RELATIVE FOLDING FREE ENERGY IN COM- POS348 BINATORIAL SEQUENCE SPACES OF T4 LYSOZYME PROTEASE ACTIVITIES IN UNFERTILIZED AND FERTILIZED EGGS AND EARLY Ryan Hayes (1), Charles Brooks III LARVAE OF PINK SALMON, O. GORBUSCHA (1) University of Michigan (Ann Arbor, United States) Liudmila Lysenko (1), Nadezda Kantserova, Nina Nemova (1) Institute of Biology, KarRC RAS (Petrozavodsk, Russia) POS342 MOLECULAR MECHANISM OF BACTERIAL HSP90 PH-DEPENDENT ATPASE POS349 ACTIVITY MICROFLUIDIC DIFFUSIONAL SIZING ENABLES CHARACTERISATION OF PRO- Yi Jin (1), Reyal Hoxie, Timothy Street TEIN-PROTEIN INTERACTIONS UNDER NATIVE CONDITIONS (1) Ms (Waltham, United States); (2) Dr (Waltham, United States) Chris Thorne (1), Sean Devenish, Tom Scheidt, Jackie Carozza, Paolo Aro- sio, Yingbo Zhang, Alexander Buell, Thomas Müller, Andrew Lynn, Jona- POS343 than Faherty, Maya Wright, Maren Butz, Tuomas Knowles IDENTIFYING DRUG BINDING SITES FROM SURFACE CONSERVATION AND (1) Fluidic Analytics (Cambridge, United Kingdom) FRAGMENT DOCKING Ho Leung Ng (1) (1) Kansas State University (Manhattan, United States)

134 135 POS356 #PS32 NEW ENGINEERED PROTEIN-G VARIANTS BINDING HUMAN KAPPA AND Posters LAMBDA SCAFFOLDS POS350 Tomasz Slezak (1), Lucas Bailey, Kelly O'Leary, Elena Davydova, Anthony BOSE: THE FUNCTIONAL LOW FREQUENCY MODES OF VERY LARGE SYSTEMS Kossiakoff WITH ATOMIC ACCURACY USING BLOCKS OF SELECTED ELASTICITY, AND ITS (1) Department of Biochemistry and Molecular Biology, The University of APPLICATION TO HIV-1 CAPSID Chicago (Chicago, United States) Hyuntae Na (1), Guang Song (1) Penn State Harrisburg (Middletown, United States) POS357 MOLECULAR INSIGHT OF THERMAL BEHAVIOR OF A BACILLUS SUBTILIS LIPASE POS351 BY PROTEIN ENGINEERING ANTIBODY ENGINEERING FACILITATED BY AVIDITY Shelly Goomber (1), Jagdeep Kaur Agnieszka Jendroszek (1), Magnus Kjærgaard (1) (1) National Institute of Malaria Research (New Delhi, India) (1) Aarhus University (Aarhus, Denmark) POS358 POS352 EXPLORING THE LIGAND EFFICACY OF CANNABINOID RECEPTOR 1 (CB1) PROTECTIVE ROLE OF VITAMIN K3 AGAINST PROTEIN AGGREGATION: IMPLI- USING MOLECULAR DYNAMICS SIMULATIONS CATION IN THE TREATMENT OF NEURODEGENERATION Wookyung Yu (1), Sang Won Jung, Art Cho Rizwan Khan (1), Parvez Alam (1) DGIST (Daegu, South Korea) (1) Aligarh Muslim University, India (Aligarh, India) POS359 POS353 MOLECULAR MODELLING AND EXPERIMENTAL STUDIES OF A FUNDER MU- STRUCTURAL CHARACTERIZATION OF THE HUMAN ASTROVIRUS (HASTV) TO TATION CAUSING HOMOCYSTINURIA IN QATAR - STRUCTURAL BASIS FOR INVESTIGATE THE PROTEASE MEDIATED VIRAL MATURATION PROCESS DEVELOPMENT OF NOVEL THERAPIES Matthew Ykema (1), Meng Xun, Yizhi Tao Navaneethakrishnan Krishnamoorthy (1), Hesham Ismail, Gheyath Nasrallah (1) Rice University (Houston, United States) (1) Systems Biology, Sidra medical and Research Center (Doha, Qatar)

POS354 POS360 HEME METALLOPROTEINS AS POTENTIAL TARGETS FOR MODIFICATIONS BY A TINY INSECTICIDAL PROTEIN LIKELY EMPLOYS DIMERIZATION TO PROTECT HOMOCYSTEINE ITS INTEGRITY IN SOLUTION Gurumayum Suraj Sharma (1), Laishram R Singh Brian Gibbons (1) (1) Dr. B.R. Ambedkar Centre for Biomedical Research, University of Delhi (1) Corteva Agriscience, Agriculture Division of DowDuPont (Hayward, (Delhi, India) United States)

POS355 POS361 N-TERMINAL AMINO ACID IDENTIFICATION USING CHAPERONE-LIKE MOLECULES PROTEIN INTERACTION NETWORK OF POLΖ IN S. CEREVISIAE Nicholas Callahan (1), Jennifer Tullman, Ben Ellington, Morgan O'Brien, Kerry Silva (1), Dmitry Korzhnev (1) McKenzie Christiensen, Zvi Kelman John Marino (1) UCONN Health (Farmington, United States) (1) University of Maryland (Rockville, United States) POS362 STRUCTURAL AND BIOPHYSICAL CHARACTERIZATION OF HUMAN KERA- TIN-ASSOCIATED PROTEINS (KAPS) Othman Rechiche (1), Jeff Plowman, Duane Harland, Verne Lee, Shaun Lott (1) University Of Auckland (Auckland, New Zealand) 136 137 #PS32 Posters POS369 A CHEMOENZYMATIC APPROACH FOR THE SYNTHESIS OF MONODISPERSE POS363 HIGHER MOLECULAR WEIGHT HEMOGLOBINS BALANCING KINETIC AND THERMODYNAMIC BARRIERS TO ISOMERIZATION Johann Sigurjonsson (1), John Antos, Spencer Anthony-Cahill CATALYSIS IN PROBIOTIC LACTOBACILLUS PLANTARUM (1) Western Washington University (Bellingham, United States) Josef Bober (1), Nikhil Nair (1) Tufts University (Medford, United States) POS370 GFP-BASED BIOSENSOR TO DETECT TRANSIENTLY EXPRESSED PROTEINS POS364 Matthew Eason (1), Antonia Pandelieva, Safwat Khan, Guido Calderini, PROTEIN LYSINE ACETYLATION, MALONYLATION, SUCCINYLATION, CROTO- Hernan Garcia, Roberto Chica NYLATION, AND 2-HYDROXYISOBUTYRYLATION IN DEVELOPING RICE SEED (1) University of Ottawa (Ottawa, Canada) AND THEIR ROLES IN SEED METABOLIC REGULATION AND NUTRIENT RESER- VOIR DEVELOPMENT POS371 Zhaohua Peng (1) STRUCTURE-BASED MODELING OF FLUORESCENCE LEVELS IN GREEN FLUO- (1) Mississippi State University (Mississippi State, United States) RESCENT PROTEIN FROM AEQUOREA VICTORIA UPON SINGLE AND MULTIPLE AMINO ACID SUBSTITUTIONS POS365 Majid Masso (1) CHARACTERISATION OF PROTEIN COMPLEXES ESSENTIAL TO CELLULAR (1) George Mason University (Manassas, United States) TRAFFICKING Emma Livingstone (1), Andrew Whitten, Saroja Weeratunga, Jennifer POS372 Martin, Brett Collins MAPPING BETA TURN GEOMETRY AND ITS SIDE-CHAIN DETERMINANTS (1) Institute for Molecular Bioscience, The University of Queensland (Bris- Nicholas Newell (1) bane, Australia) (1) Newell (Reading, United States)

POS366 POS373 SYNTHESIS OF TITANIUM-BINDING CXCL12 VARIANTS BY EXPRESSED PROTEIN DEFINING STRUCTURAL MECHANISM OF CARBOHYDRATE RECOGNITION BY SEX4 LIGATION FOR IMPROVED OSSEOINTEGRATION OF BONE IMPLANTS Madushi Raththagala (1), Jordan Alvarez, Craig Vander Kooi, Matthew Sabrina Spiller (1), Nydia Panitz, Annette Beck-Sickinger Gentry (1) Leipzig University, Institute of Biochemistry (Leipzig, Germany) (1) Skdimore College (Saratoga Springs, United States)

POS367 POS374 NOVEL MECHANISMS OF HSF1 ACTIVITY REVEALED BY DEEP MUTATIONAL DEFINING THE SUBSTRATE SPECIFICITY OF GLUCAN PHOSPHATASE IN RE- SCANNING VERSIBLE STARCH PHOSPHORYLATION Michael Dorrity (1), Elizabeth Morton, Stanley Fields, Christine Queitsch Claudia Mak (1), Madushi Raththagala (1) Department of Genome Sciences, University of Washington (Seattle, (1) Skdimore College (Saratoga Springs, United States) United States) POS375 POS368 STUDYING CONFORMATIONAL HETEROGENEITY OF BIOMOLECULES USING CRISPR-CAS9 MEDIATED DNA UNWINDING DETECTED USING SITE-DIRECTED TRAVELING WAVE ION MOBILITY ARRIVAL TIME DISTRIBUTION WIDTH AND SPIN LABELING MOLECULAR DYNAMICS SIMULATIONS Peter Qin (1), Narin Tangprasertchai, Rosa Di Felice, Xiaojun Zhang, Ian Sugyan Dixit (1), Brandon Ruotolo Slaymaker, Carolina Vazquez Reyes, Wei Jiang, Remo Rohs (1) University of Michigan (Ann Arbor, United States) (1) Univeristy of Southern California (Los Angeles, United States) 138 139 #PS32

POS382 Posters FUNCTIONAL ASSIGNMENT OF STRUCTURAL GENOMICS PROTEINS THROUGH COMPUTED CHEMICAL PROPERTIES, GRAPH REPRESENTATION OF ACTIVE POS376 SITES, AND BIOCHEMICAL VALIDATION ADDRESSING CHALLENGES IN RECOMBINANT PROTEIN PRODUCTION USING Caitlyn Mills (1), Rohan Garg, Joslynn Lee, Ramya Parasuram, Liang Tian, CELL FREE EXPRESSION Alexandru Suciu, Gene Cooperman, Penny Beuning, Mary Jo Ondrechen Jennifer Hardman (1), Renee Mille), Jennifer DiMauro, Mark Michalak, (1) Northeastern University (Boston, United States) Silvino Sousa, Bernhard Sielaff, Medha Tomlinson (1) AbbVie Bioresearch Center (Worcester, United States) POS383 METAL-CONTROLLED PROTEIN DIMERIZATION POS377 Brian Maniaci (1), Boguslaw Stec, Tom Huxford, John Love THE ROLE OF HELICITY IN THE SELF-ASSEMBLY OF THE C-TERMINAL DOMAIN (1) San Diego State University (San Diego, United States) OF TDP-43 Alexandra D'Ordine (1), Alexander Conicella, Nicolas Fawzi POS384 (1) Brown University (Providence, United States) STRUCTURAL INSIGHTS INTO THE IMPACT OF TWO HOLOPROSENCEPHALY-RE- LATED MUTATIONS AND THE DNA-BINDING MECHANISM OF HUMAN TGIF1 POS378 HOMEODOMAIN THE STRUCTURAL BASIS FOR CANCER DRUG INTERACTIONS WITH THE CATA- Maili Liu (1), Shuangli Li LYTIC AND ALLOSTERIC SITES OF SAMHD1 (1) Wuhan Institute of Physics and Mathematics, Chinese Academy of Kirsten Knecht (1), Olga Buzovetsky, Constanze Schneider, Dominique Sciences (Wuhan, China) Thomas, Vishok Srikanth, Florentina Tofoleanu, Krystle Reiss, Nerea Ferreiros, Gerd Geisslinger, Victor Batista, Xiaoyun Ji, Jindrich Cinatl Jr., Oliver T. POS385 Keppler, Yong Xiong STRUCTURAL INSIGHTS INTO ADP-DEPENDENT GLUCOKINASE MECHANISM (1) Yale University (New Haven, United States) OF CATALYSIS AND INHIBITION Przemysław Grudnik (1), Marcin Kaminski, Krzysztof Rembacz, Piotr Tokarz, POS379 Katarzyna Kuska, Magdalena Wisniewska, Maciej Dawidowski, Mariusz ISOTHERMAL DNA ASSEMBLY TOOLS FOR GENERATING PROTEIN DIVERSITY Madej, Jan Potempa, Grzegorz Dubin AND FACILITATING RECOMBINANT STRAIN CONSTRUCTION (1) Jagiellonian University, Malopolska Centre of Biotechnology (Krakow, Ryan Heller (1), Katarzyna Crissy, Thomas Schoenfeld Poland) (1) QIAGEN (Beverly, United States) POS386 POS380 MODELING THE INTERACTIONS OF HUMAN XPA AND RPA IN ROSETTA PROTEOME-SCALE RELATIONSHIPS BETWEEN LOCAL AMINO ACID COMPOSI- John Cordoba (1), Agnieszka Topolska-Wos, Kateryna Ogorodnik, Rocco TION AND PROTEIN FATES AND FUNCTIONS Moretti, Daniel Rosenberg, Michal Hammel, Jens Meiler, Walter Chazin Sean Cascarina (1), Eric Ross (1) Vanderbilt University (Nashville, United States) (1) Colorado State University (Fort Collins, United States) POS387 POS381 ENGINEERING AND SUBSTRATE SPECIFICITY OF FT_T: AN OPTIMIZED VERSION PHYSICAL POWER GENERATION MECHANISM OF ROTARY MOLECULAR MOTOR OF RTDA F1-ATPASE BY STATIC AND DYNAMIC X-RAY CRYSTALLOGRAPHIC STUDIES Stephen Duff (1), Clayton Larue, Michael Goley, Lei Shi, Artem Evdokimov, Toshiharu Suzuki (1), Kunio Hirata, Eiki Yamashita, Seiki Baba, Naoya Iida, Takashi Oscar Sparks, Christine Ellis, Andrew Wallacott Timothy Rydel, Coralie Halls, Kumasaka, Toshiya Endo, Toru Hisabori, Masasuke Yoshida, Hiroyuki Noji Brook Van Scoyoc, Jeffrey Nageotte, Xiaoran Fu, Adewale Adio, Jeffrey (1) Department of Applied Chemistry, School of Engineering, The University Haas, Meiying Zheng of Tokyo (Tokyo, Japan) (1) Monsanto Co. (St. Louis, United States) 140 141 #PS32 Posters POS394 DYNAMICS OF REDOX TERNARY COMPLEX IN THE CYTOCHROME P450 METABOLON IS MODULATED BY SUBSTRATE BINDING: AN NMR STUDY POS388 Katherine Gentry (1), Meng Zhang, Sang-Choul Im, Lucy Waskell, Ayyalu- PROBING THE INTERACTION BETWEEN SERINC3 AND CLATHRIN ADAPTOR samy Ramamoorthy PROTEIN AP-2 (1) University of Michigan (Ann Arbor, United States) Christopher Lim (1), Rajendra Singh, John Guatelli, Yong Xiong POS395 (1) Yale University (NEW HAVEN, United States) X-RAY STRUCTURE OF MERS PAPAIN-LIKE PROTEASE BOUND WITH ISG15 FACILITATES DESIGN OF PLPS WITH ATTENUATED OR ENHANCED SUBSTRATE POS389 SPECIFICITIES ORTHOGONAL EXPRESSION OF AN ARTIFICIAL METALLOENZYME FOR ABIOTIC Jozlyn Clasman (1) CATALYSIS (1) Purdue University (West Lafayette, United States) Timothy Schwochert (1), Evan Reynolds, Matthew McHenry, John Watters, Eric Brustad POS396 (1) UNC Chapel Hill (Carrboro, United States) TITLE: MASS SPECTROMETRY BASED PROTEOMICS TO INVESTIGATE THE MOLECULAR CHANGES IN RAT ATRIA DURING OBSTRUCTIVE SLEEP APNEA POS390 Devika Channaveerappa (1), Jacob Lux, Meredith McLerie, Brian Pana- DEVELOPMENT OF A SPR ASSAY FOR DETERMINING THE BINDING AFFINITY ma, Costel Darie OF SMALL MOLECULES TO TAU AGGREGATES (1) Clarkson University (POTSDAM, United States) Andreia Serra (1), Christopher Delgado, Patrick Rodriguez, Emanuele Gabellieri, Francesca Capotosti, Heiko Kroth, Chary Nampally, David Hick- POS397 man, Andreas Muhs, Andrea Pfeifer 3D FOLDING FROM MUTATION SCANNING (1) AC Immune (Lausanne, Switzerland) Kelly Brock (1), Nathan Rollins, Frank Poelwijk, Michael Stiffl er, Nicholas Gauthier, Chris Sander, Debora Marks POS391 (1) Harvard Medical School (Cambridge, United States) STRUCTURE AND INHIBITION OF THEM2, AN ACYL-COA THIOESTERASE THAT CONTROLS HEPATIC GLUCOSE AND LIPID METABOLISM POS398 Xu Liu (1), Veronika Tillander, David Cohen, Eric Ortlund STRUCTURAL INSIGHTS ON PHENAZINE M IN COMPLEX WITH ITS COFACTOR (1) Emory University (Atlanta, United States) S-ADENOSYL-L-METHIONINE Thamires Froes (1), Marcelo Castilho, Carla Mattos POS392 (1) Northeastern University (Boston, United States) PRODUCTION OF SUBUNIT VACCINE CANDIDATES AGAINST BOVINE RESPIRATORY DISEASE PATHOGEN MANNHEIMIA HAEMOLYTICA AS AN POS399 ALTERNATIVE TO ANTIMICROBIALS SEARCHING FOR FOLDING PATHWAYS OF TRP-CAGE Angelo Kaldis (1), Trevor Alexander, Rima Menassa Qingzhe Tan (1), Minghai Li, Shuanghong Huo, Li Han (1) Agriculture and Agri-Food Canada (London, Canada) (1) Clark University (Worcester, United States)

POS393 POS401 AMYLOID AGGREGATION OF HIAPP, HCT AND AΒ ALTERED BY A WATER CREATING A LIBRARY OF FUNCTIONAL DE NOVO PROTEINS ON A STABLY SOLUBLE CURCUMIN DERIVATIVE FOLDED STRUCTURAL TEMPLATE Sarah Cox (1), Diana C. Rodriguez Camargo, Young-Ho Lee, Magdalena Christina Karas (1) I. Ivanova, Bernd Reif, Ayyalusamy Ramamoorth (1) Princeton University (Princeton, United States) (1) University of Michigan (Ann Arbor, United States) 142 143 #PS32 Posters POS408 SMALL MOLECULE STABILIZERS OF AMYLOIDOGENIC ANTIBODY LIGHT CHAINS POS402 Gareth Morgan (1), Nicholas Yan, Jeffery Kelly, Lewis Kay, Enrico Rennella PROTEIN CONFORMATIONAL TRANSITIONS FROM ALL-ATOM ADAPTIVELY (1) The Scripps Research Institute (LA JOLLA, United States) BIASED PATH OPTIMIZATION (ABPO) Heng Wu (1), Carol Post POS409 (1) Purdue University (West Lafayette, United States) MODELING TUBULIN E-HOOKS INTERACTIONS WITH DYNEIN MICROTUBULE BINDING DOMAIN POS403 Nayere Tajielyato (1), Joshua Alper, Emil Alexov STABILITY OF SINGLE DOMAIN ANTIBODIES ESTIMATED BY MOLECULAR (1) Clemson university (Clemson, United States) DYNAMICS SIMULATION Narutoshi Kamiya (1), Benson Ma, Gert-Jan Bekker POS410 (1) University of Hyogo (Kobe, Japan) TRYPSIN-CATECHIN: A NOVEL COMPLEX AND ANTIOXIDANT FUNCTIONS Idania Quintero (1), María Jesús Moreno Vázquez, Manuel Ignacio Carre- POS404 tas Valdez, Abril Zoraida Graciano Verdugo, Aldo Alejandro Arvizu Flores MOLECULAR CHARACTERIZATION OF SINGLE-CHAIN ANTIBODY VARIABLE (1) Universidad de Sonora (Hermosillo, Mexico) FRAGMENTS (SCFV) SPECIFIC TO TWO PNEUMOCOCCAL ANTIGENS Sangho Lee (1), Dongho Lee, Soobin Park, ShinA Jang, Jihye Oh, Seungsu POS411 Han, Gyuhee Kim, Seungyeop Lee, Prachetash Ghosh, Dong-Kwon Rhee IMPLEMENTATION OF N-LAUROYLSARCOSINE SODIUM SALT TO INCREASE (1) Sungkyunkwan University (Suwon, South Korea) THE YIELD OF RECOMBINANT TRYPSIN I OF MONTEREY SARDINE (SARDINOPS SAGAX CAERULEA) POS405 Dania Rodríguez (1), Idania Quintero, Aldo Arvizu, Manuel Carretas, Rocio ELUCIDATING THE MECHANISM OF C-S BOND CLEAVAGE IN ISETHIONATE Sugich SULFITE-LYASE (1) University of Sonora (Obregón , Mexico) Christopher Dawson (1), Spencer Peck, Stephania Irwin, Emily Balskus, Catherine Drennan POS412 (1) Department of Biology, Massachusetts Institute of Technology, Cam- STRUCTURE OF CASEIN KINASE 1Α AS A TOOL IN RATIONAL DRUG DESIGN bridge, MA 02139, USA (Cambridge, United States) Kasia Handing (1), Steven M. Corsello, Eric Stefan, Isaline Castan, Rohith Nagari, Sara Gelles-Watnick, Jennifer Gale, Virendar Kaushik, Robert POS406 Hilgraf, Carol Mulrooney, Karen Emmith, Chris Lemke, Colin Garvie, Todd NON-RIBOSOMAL PROTEIN SURF6 ENABLES SEAMLESS REORGANIZATION IN R. Golub NPM1-DEPENDENT NUCLEOLAR NETWORKS (1) Broad Institute (Cambridge, United States) Mylene Ferrolino (1),Diana Mitrea, J. Robert Michael, Richard Kriwacki (1) St. Jude Children's Research Hospital (Memphis, United States) POS413 IDENTIFICATION OF POTENTIAL INHIBITORS OF THE SIGMA-28 TRANSCRIP- POS407 TION FACTOR FULL-LENGTH RECOMBINANT HUMAN TYROSINASE & TYROSINASE-RELATED Sabrina Apel (1), Julie Pieslak, Sharon Shechter, Mattthew Gage PROTEIN 1: SIMILAR STRUCTURE, DIFFERENT FUNCTION (1) University of Massachusetts Lowell (Revere, United States) Kenneth L. Young II (1), Monika B. Dolinska, Paul T. Wingfi eld, Eugenia Poliakov, Yuri V. Sergeev (1) National Eye Institiute, National Institutes of Health (Bethesda, United States) 144 145 POS420 #PS32 Posters OBSERVING THE DOMINANT TRANSITION PATH OF ELONGATION FACTOR G DURING TRANSLOCATION POS414 Osmaan Shahid (1), Paul Whitford (2) BIOCHEMICAL AND BIOPHYSICAL CHARACTERIZATION OF NUCLEOSIDE (1) Northeastern University (Highland, United States); (2) Department of DIPHOSPHATE KINASE FROM WHITE SHRIMP (LITOPENAEUS VANNAMEI Physics, Northeastern University (Boston, United States) Ana Elizabeth Ureña (1), Idania Quintero, Rocio Sugich, Aldo Arvizu, En- rique Velazquez, Francisco Castillo, Rogerio Sotelo POS421 (1) University of Sonora (Obregon, Mexico) MULTI-MAPPING READS IN RIBOSOME PROFILING Jackson Halpin (1), Radhika Jangi, Timothy Street POS415 (1) Brandeis University (Waltham, United States) MODIFIED TRANSLATIONALLY CONTROLLED TUMOR PROTEIN-DERIVED PRO- TEIN TRANSDUCTION DOMAIN ENHANCES NASAL DELIVERY OF PEPTIDES POS422 Moonhee Kim (1), Hae-duck Bae, Joohyun Lee, Kyunglim Lee EXPLORATION OF COILED-COIL SPECIFICITY WITH A MULTIPLEXED SYSTEM (1) Ewha Womans University (Seoul, South Korea) FOR ASSAYING PROTEIN-PROTEIN INTERACTIONS William Boldridge (1), Ajasja Lubetic, Hwangbeom Kim, Nate Lubock, POS416 Roman Jerala, Sriram Kosuri COMPARABILITY, SIMILARITY, LINEARITY AND HIGH ORDER STRUCTURE ANAL- (1) Department of Chemistry and Biochemistry University of California, Los YSIS OF AN IGG1 SAMPLE BY MICROFLUIDIC MODULATION SPECTROSCOPY Angeles (LOS ANGELES, United States) Libo Wang (1), Lucy Liu, Jason Rouse, Eugene Ma, Jeffery Zonderman (1) RedShift Bioanalytics (Burlington, United States) POS423 STRUCTURAL AND MECHANISTIC STUDIES OF THE ANTIBIOTIC, ARGYRIN B POS417 Chris Swanson (1), Catie Shelton, Riley Roberts, Tanner Thuet-Davenport, STRUCTURE DETERMINATION OF A BIOENGINEERED HUMAN/PORCINE Clint Spiegel FACTOR VIII FOR HEMOPHILIA A TREATMENT, AND IMPROVEMENTS TO THE (1) Western Washington University (Bellingham, United States) HUMAN FACTOR VIII MODEL Ian Smith (1), Clint Spiegel POS424 (1) Western Washington University (Bellingham, United States) A TRIANGULAR PROTEIN NANOSTRUCTURE CREATED BY MODULAR FUSION AND ASSEMBLY OF SYNTHETIC HETERODIMERIC COILED COILS POS418 Won Min Park (1), Mostafa Bedewy, Karl Berggren, Amy Keating STRUCTURAL AND MECHANISTIC STUDIES OF THE IMMUNE RESPONSE TO THE (1) MIT, Department of Biology (Cambridge, United States) BLOOD COAGULATION FACTOR VIII C1 DOMAIN Shaun Peters (1), Robert Johnson, Paul C. Spiegel POS425 (1) Western Washington University (Bellingham , United States) THE FLEXIBLE LINKER BETWEEN THE TRANSACTIVATION AND DNA-BINDING DOMAINS OF IRF3 IS NOT CRITICAL FOR IFNΒ INDUCTION POS419 Anne Jecrois (1), Nese Kurt-Yilmaz), Celia Schiffer), William Royer MULTIMERS OF CU/ZN SUPEROXIDE DISMUTASE IN CYTOPLASMIC EXTRACTS (1) University of Massachusetts Medical School (Worcester, United States) OF MUSSEL GILL AND MANTLE TISSUES Mary Hamilton (1) POS426 (1) Fordham University (New York, United States) FILMING PROTEIN-LIGAND INTERACTIONS AT SINGLE MOLECULAR LEVEL IN REAL-TIME WITH CLYA NANOPORES Xin Li (1), Kuo Hao Lee, Jianhan Chen Min Chen (1) University of Massachusetts Amherst (Amherst, United States) 146 147 POS433 #PS32 Posters MOLECULAR DYNAMICS STUDY FOR POTENTIAL ABL TYROSINE KINASE POS427 INHIBITORS DERIVED FROM 2-PYRAZOLINYL-1-CARBOTHIOAMIDE CHARACTERIZATION OF SMALL MOLECULES THAT MODULATE ERAP1 ACTIVI- Beom Soo Kim (1), Sang Won Jung, Yoongho Lim, Wookyung Yu TY BY AFFECTING ITS CONFORMATIONAL DYNAMICS (1) DGIST (Daegu, South Korea) Richa Arya (1), Zachary Maben, Lawrence Stern (1) University of Massachusetts Mediccal School (Worcester, United States) POS434 MECHANISM OF MULTIDRUG RESISTANCE TRANSCRIPTIONAL REGULATION POS428 REVEALED BY DYNAMIC ANALYSIS USING NMR METABOLIC AND PROTEOLYTIC ENZYME ACTIVITIES IN THREESPINE STICKLE- Koh Takeuchi (1) BACK GASTEROSTEUS ACULEATUS OF THE WHITE SEA (1) National Institute for Advanced Industrial Science and Technology Maria Churova (1), Liudmila Lysenko, Nadezda Kantserova, Natalia Shulgina, (Tokyo, Japan) Nina Nemova (1) Institute of Biology of the Karelian Research Centre of the Russian POS435 Academy of Sciences (Petrozavodsk, Russia) INSECT IMP-L2 PROTEIN STRUCTURE AND THERMODYNAMICS PRESENTS NEW MOLECULAR STRATEGY FOR THE REGULATION OF BIO-AVAILABILITY OF INSU- POS429 LIN-LIKE HORMONES CONFORMATIONAL FLEXIBILITY IS CRITICAL FOR CATALYTIC ACTIVITY OF Cristina Viola (1), Marek Brzozowski DENGUE VIRUS NS2B-NS3 PROTEASE (1) University of York (York, United Kingdom) Maureen Hill (1), Jeanne Hardy (1) University of Massachusetts Amherst (Amherst, United States) POS436 ENGINEERING A FRET-BASED BIOSENSOR FOR IN-SITU DETECTION OF D-SERINE POS430 Vanessa Vongsouthi (1), Jason Whitfi eld, Colin Jackson DESIGNING SCAFFOLDED ARTEMIN AND GDNF PEPTIDE DIMERS TO INVESTIGATE (1) Research School of Chemistry, Australian National University (Canberra, THE MECHANISM OF ACTIVATION OF THE RET RECEPTOR TYROSINE KINASE Australia) Paula Ortet (1), Melesilika Finau (1) Graduate program in Molecular Biology, Cell Biology and Biochemistry, POS437 Boston University (MALDEN, United States) ROLE OF THE FACIAL TRIAD IN FACTOR INHIBITING HIF (FIH): LIGAND BIND- ING AND UNCOUPLING POS431 Vanessa Chaplin (1), Michael Knapp PROBING MECHANICAL PROPERTIES OF PROTEINS AND TRNA USING (1) University of Massachusetts Amherst (AMHERST, United States) NANOPORES Prasad Bandarkar (1), Robert Henley, Huan Yang, Meni Wanunu, Paul Whitford POS438 (1) Northeastern University (Brighton, India) INVESTIGATING THE IMPORTANCE OF DISTAL RESIDUES IN PARKIN Jenifer Winters (1), Penny J. Beuning, Lee Makowski, Mary Jo Ondrechen POS432 (1) Northeastern University (Allston, United States) SILK FIBROIN NANOCRYSTALS FOR REINFORCING HYDROGEL NETWORK Ki Hoon Lee (1), Jungsoo Kim POS439 (1) Seoul National University (Seoul, South Korea) EFFECTS OF DIETARY INCLUSION OF DIHYDROQUERCETIN ON PROTEIN OXI- DATION, CALPAIN AND PROTEASOME ACTIVITY LEVELS IN RAINBOW TROUT SKELETAL MUSCLES AND LIVER Nadezda Kantserova (1), Liudmila Lysenko, Ekaterina Tushina (1) Institute of Biology of Karelian Research Centre of Russian Academy of Sciences (Petrozavodsk, Russia) 148 149 #PS32 POS446 Posters THE ROLE OF FURIN IN THE INTOXICATION PATHWAY OF PSEUDOMONAS POS440 EXOTOXIN A BASED RECOMBINANT IMMUNOTOXINS ILLUMINATING THE PATH FROM FATTY ACYL-COA SYNTHETASES TO LUCIFERASES Brian Grossman (1), Jack Sanford, Yuyi Zhu, Nathaniel Donahue, Bryan Spencer Adams Jr. (1), Stephen Miller (1) Miller, John Weldon (1) University of Massachusetts Medical School (Worcester, United States) (1) Towson University (Baltimore, United States)

POS441 POS447 APPLYING FRUSTRATION ANALYSIS TO PREDICT FUNCTIONAL DOMAINS IN TWO STRUCTURAL MOTIFS DETERMINE MEMBRANE TOPOLOGY ADENO-ASSOCIATED VIRUS CAPSID ASSEMBLY AND DISASSEMBLY Sonya Entova (1), Jean-Marc Billod, Jean-Marie Swiecicki, Sonsoles Mar- Nicole Thadani (1), Kiara Reyes Gamas, Susan Butler, Peter Wolynes, Junghae tin-Santamaria, Barbara Imperiali Suh (1) Massachusetts Institute of Technology (Cambridge, United States (1) Rice University (Houston, United States) POS448 POS442 BALANCE OF CONFORMATIONAL STATES AFFECTS INTRINSIC HYDROLYSIS OF PROTEIN DEGRADATION AS A MECHANISM OF OSMOLARITY MAINTENANCE NRAS AND ITS ONCOGENIC MUTANTS IN MARINE ORGANISMS Derion Reid (1), Carla Mattos Liudmila Lysenko (1), Nadezda Kantserova, Elena Kaivarainen, Marina (1) Northeastern University (Boston, United States) Krupnova, Nina Nemova (1) Institute of Biology, KarRC RAS (Petrozavodsk, Russia) POS449 BROWNIAN DYNAMICS STUDY OF THE EFFECT OF PROTEIN SIZE ON PROTEIN POS443 DIFFUSION THROUGH THE NUCLEOID STRUCTURAL CHARACTERIZATION OF THE INSULIN-DEGRADING ENZYME BY Benson Ma (1) MICROFLUIDIC MODULATION SPECTROSCOPY (1) Georgia Institute of Technology (Atlanta, United States) Valerie Ivancic (1), Libo Wang, Eugene Ma, Noel Lazo (1) RedShift BioAnalytics (Burlington, United States) POS450 AN EXPLORATION OF AN RGS-LOV-DUF TRI-DOMAIN PROTEIN: GAINING POS444 BIOPHYSICAL INSIGHTS INTO NEW BLUE LIGHT-CONTROLLED MECHANISMS RECORDING THE FITNESS LANDSCAPES OF SMALL DELETIONS AND SUBSTITU- FOR CELL SIGNALING TIONS IN THE GREEN FLUORESCENT PROTEIN Zaynab Jaber (1), Spencer Glantz, Erin Berlew, Brian Y. Chow, Kevin H. Maya Petek (1), Stephane Emond, Florian Hollfelder Gardner (1) University of Cambridge (Cambridge, United Kingdom) (1) Structural Biology Initiative, CUNY Advanced Science Research Center, New York, NY 10031 AND Ph.D. Program in Biochemistry, The Graduate POS445 Center of the City University of New York, New York, NY 10016 (New York, TARGETING UBIQUITIN INTERACTING MOTIFS WITH ENGINEERED UBIQUITINS United States) TO MODULATE CANCER CELL PROLIFERATION Gianluca Veggiani (1), Bradley Yates, Sachdev Sidhu POS451 (1) University of Toronto (Toronto, Canada) PREDICTING ALTERNATIVE CONFORMATIONS OF MEMBRANE PROTEINS USING EVOLUTIONARY SEQUENCE INFORMATION Jung-Eun Shin (1), Debora Marks (1) Harvard University (Cambridge, United States)

150 151 #PS32 POS459 Posters MODULATION OF GLUTAMATE DEHYDROGENASE 1 ALLOSTERY Erica Johnson (1), Mary Konkle, Chimere Nnatubeugo, Michael Menze POS452 (1) Ball State University (Muncie, United States) STUDYING THE MOLECULAR BASIS OF INHIBITOR POTENCY IN HIV-1 PROTE- ASE USING A DATA DRIVEN BIOINFORMATICS APPROACH POS460 Florian Leidner (1), Celia Schiffer ANALYSIS OF CIRCULATING MIRNAS BY MICROARRAY IN SYSTEMIC SCLEROSIS (1) University of Massachusetts Medical School (Worcester, United States) Marta Rusek (1), Małgorzata Michalska-Jakubus Małgorzata Kowal, Jerzy Bełtowski, Dorota Krasowska POS453 (1) Medical University of Lublin (Lublin, Poland) INVESTIGATING LOW INPUT DETECTION IN QUANTITATIVE PCR Megan Hill (1), Gregory Patton, Nicole Nichols POS461 (1) New England Biolabs (Ipswich, United States) INSIGHTS ON THE GΑ:RIC8A INTERACTION Levi McClelland (1), Stephen Sprang, Tung-Chung Mou, Baisen Zeng POS454 (1) University of Montana (Missoula, United States) KINETIC CHARACTERIZATION OF AN ULTRA-HIGH FIDELITY DNA POLYMERASE Kinjal Dave (1), Andrew Gray, Nicole Nichols POS463 (1) New England Biolabs (Ipswich, United States) EARLY EVENTS IN AMYLOID FORMATION BY LYSOZYME DETECTED BY MICRO- FLUIDIC MODULATION SPECTROSCOPY POS455 Qiuchen Zheng (1), Valerie Ivancic, Libo Wang, Eugene Ma, Noel Lazo FUNCTIONAL ANNOTATION OF ENZYMES IN THE HALOACID DEHALOGENASE (1) Clark University (Worcester, United States) SUPERFAMILY BY COMPUTATIONAL AND BIOCHEMICAL METHODS Lydia Ruffner (1), Mong Mary Touch, Penny Beuning, Mary Jo Ondrechen POS464 (1) Northeastern University (Boston, United States) ANALYZING MUTATIONS IN HUMAN ΓD CRYSTALLIN USING HIGH THROUGH- PUT THERMAL STABILITY SHIFT ASSAYS POS456 Ishara Mills-Henry (1), Colin O'Neil, Kene Piasta, Melissa Kosinski-Collins DEVELOPMENT OF MACROCYCLE-SPECIFIC MOLECULAR DESCRIPTORS AND (1) Framingham State University (Framingham, United States) THEIR APPLICATION IN MACHINE LEARNING Lauren Viarengo (1), Adrian Whitty POS465 (1) Boston University, Department of Chemistry (Boston, United States) HOW DO THE ER CHAPERONES BIP AND GRP94 HELP FOLD INSULIN-LIKE GROWTH FACTORS? POS457 Judy Kotler (1), Timothy Street CHARACTERIZATION AND APPLICATIONS OF 5-METHYL-CYTOSINE INCOR- (1) Brandeis University (Waltham, United States) PORATION VIA PCR Joseph McGaunn (1), Andrew Gray, Nicole Nichols POS466 (1) New England Biolabs (Ipswich, United States) STRUCTURE OF TIP20, A SUBUNIT OF THE DSL1 TETHERING COMPLEX, BOUND TO ITS COGNATE SNARE REVEALS A MECHANISM FOR PROMOTING SNARE ASSEMBLY POS458 Sophie Travis (1), Frederick Hughson PREPARATION OF D48N/K116Q MUTANT OF LYSOZYME WITH CHANGED (1) Princeton University, Department of Molecular Biology (Princeton, DIPOL MOMENT AND ITS INTERACTIONS WITH N-ACETYLCHITOTRIOSE United States) Beata Wielgus-Kutrowska (1), Jan Antosiewicz (1) Department of Biophysics, Institute of Experimental Physics, Faculty of Physics, University of Warsaw (Warsaw, Poland) 152 153 #PS32 POS474 Posters BIOPHYSICAL CHARACTERIZATION OF THE HSV-1 NUCLEAR EGRESS COMPLEX Mike Thorsen (1), Janna Bigalke, Elizabeth Draganova, David Hoogerhe- POS467 ide, Ekaterina Heldwein THE COORDINATED LIFE-CYCLE OF EF-TU AND TRNA ON THE RIBOSOME (1) Tufts Sackler School (Boston, United States) DURING TRNA SELECTION Justin Morse (1), Scott Blanchard POS475 (1) Weill Cornell Medical College (New York, United States) INVESTIGATING THE FUNCTIONALITY OF PROCASPASE-6 AND CASPASE-6 BY VARIOUS NUCLEOTIDES POS468 Ishankumar Soni (1) BIOCHEMICAL AND BIOPHYSICAL EXAMINATION OF THE HUMAN HECT E3 (1) Graduate Student at UMass-Amherst (Sunderland, United States) UBIQUITIN LIGASE WWP1 Emilie Ogisu (1), Donald Spratt POS476 (1) Clark University (Worcester, United States) EXPANDING THE STRUCTURAL LANDSCAPE OF INFLUENZA HEMAGGLUTININ TO INFORM VACCINE DISCOVERY EFFORTS POS469 Deb Conrady (1), Brandy Calhoun, Donald Lorimer, Peter Horanyi, Thomas STRUCTURAL AND FUNCTIONAL STUDIES OF THE HECT E3 UBIQUITIN LIGASE AREL1 Edwards Lara Prosterman (1), Donald Spratt (1) Beryllium (Bedford, United States) (1) Clark University (Worcester, United States) POS477 POS470 SYNTHETIC COLLAGEN NANOFIBERS FROM SMALL, SYMMETRICALLY DE- ACTIVATION PATHWAY DIVERSITY AS A BASIS FOR FUNCTIONAL REGULA- SIGNED PEPTIDES TION OF COAGULATION FACTOR XIII I. Caglar Tanrikulu (1), Lianna Dang, Bradley Olsen, Song Jin, Ronald Raines Boris Anokhin (1), William Dean, Muriel Maurer (1) Massachusetts Institute of Technology (Cambridge, United States) (1) University of Louisville (Louisville, United States) POS478 POS471 PHOSPHORYLATION INDUCED COCHAPERONE UNFOLDING PROMOTES KI- UNCOVERING THE CATALYTIC MECHANISM OF THE C-TERMINAL TAIL OF THE NASE RECRUITMENT AND CLIENT CLASS-SPECIFIC HSP90 PHOSPHORYLATION LARGE HECT E3 UBIQUITIN LIGASE HERC2 Vasantha Kumar Machohally Venkateshaiah (1), Dimitra Keramisanou, Noah Schwaegerle (1), Donald Spratt Ashleigh Bachman, Ioannis Gelis (1) Clark University (Worcester, United States) (1) University of South Florida (Tampa, United States) POS472 POS479 CHARACTERIZATION OF CELLULOSE DIGESTING PROTEINS FOUND IN SHIP- GARCINOLIC ACID INHIBITS TRANSCRIPTIONAL ACTIVATOR INTERACTIONS WORM SYMBIONTS WITH THE CREB BINDING PROTEIN KIX DOMAIN Samantha Watson (1), Penny Beuning, Daniel Distel, Mary Jo Ondrechen Meghan Breen (1), Omari Baruti, Matthew Beyersdorf, Stephen Joy, Sa- (1) Northeastern University (Boston, United States) mantha DeSalle, Anna Mapp (1) University of Michigan (Ann Arbor, United States) POS473 EXPLORING THE SIZE AND RESOLUTION LIMITS OF SINGLE PARTICLE POS480 CRYO-ELECTRON MICROSCOPY DEVELOPMENT OF A HIGHLY POTENT AND SPECIFIC INHIBITOR OF THE MYB- Mark Herzik (1), Mengyu Wu, Gabriel Lander KIX INTERACTION (1) The Scripps Research Institute (La Jolla, United States) Stephen Joy (1), Matthew Henley, Junius Thomas, Matthew Beyersdorf, Anna Mapp (1) University of Michigan (Ann Arbor, United States) 154 155 #PS32 POS488 Posters TOWARD STRUCTURAL UNDERSTANDING OF LIGAND RECOGNITION BY LYSO- POS481 PHOSPHATIDIC ACID RECEPTOR LPA6 PROBING THE AVIDITY EFFECT ON SABS MULTIMERIZED BY ENGINEERED PRO- Reiya Taniguchi (1), Asuka Inoue, Misa Sayama, Keitaro Yamashita, Kunio TEIN-G POLYMERS Hirata, Masahito Yoshida, Yoshiko Nakada-Nakura, Yuko Otani, Hideaki Kelly O'Leary (1), Tomasz Slezak, Katarzyna Radziwon, Elena Davydova, Kato, Tomohiro Nishizawa, Takayuki Doi, Tomohiko Ohwada, Ryuichiro Tony Kossiakoff Ishitani, Junken Aoki, Osamu Nureki (1) University of Chicago (Chicago, United States) (1) The University of Tokyo (Bunky-ku, Japan)

POS482 POS489 DISCOVERY OF ALLOSTERIC CHAPERONES TO CORRECT G6PD (GLUCOSE-6- DIFFERENT OLIGOMERIZATION PATTERNS OF PIRA AND PIRB TOXINS OF PHOSPHATE DEHYDROGENASE) DEFICIENCY VIBRIO PARAHAEMOLYTICUS AND THEIR INTERACTION WITH MEMBRANE Sunhee Hwang (1) COMPONENTS OF EPITHELIAL CELLS OF THE HEPATOPANCREAS (1) Stanford University (Stanford, United States) Marcelo Victorio-De Los Santos (1), Patricia Cano-Sánchez, Alejandra Hernández-Santoyo, Sonia Soto-Rodríguez POS483 (1) Food and Development Research Center-Mazatlán Unit (Mazatlan, CHARACTERIZATION AND ENGINEERING OF A MEMBRANE ENZYME FOR Mexico) BIOSYNTHETIC PRODUCTION OF NEW POLYMERS Bruno Motta Nascimento (1), Nikhil Nair POS491 (1) Tufts University (Medford, United States) PEPTIDE DESIGN BY OPTIMIZATION ON A HIGH-DIMENSIONAL, DATA- PARAMETERIZED PROTEIN INTERACTION LANDSCAPE POS484 Justin Jenson (1), Vincent Xue, Lindsey Stretz, Lothar Reich, Amy Keating INSIGHTS INTO ALLOSTERIC REGULATION OF HOMO-OLIGOMERIC PROTEINS (1) MIT Department of Biology (Cambridge, United States) FROM MECHANISTIC MODELING Mark Foster (1) POS492 (1) The Ohio State University (C, United States) TOWARD THE COMPUTATIONAL DESIGN OF LARIAT-TYPE MACROCYCLES TO BIND SPECIFIC PROTEIN TARGETS POS485 Kristina Streu (1), Adrian Whitty THE CONFORMATIONAL ENSEMBLE OF RAS AND ITS DIFFERENCES AMONG (1) Boston University (Boston, United States) ISOFORM AND MUTATION Alicia Volmar (1), Jillian Parker, Carla Mattos POS493 (1) Northeastern University (Boston, United States) PROBING THE HOMOTROPIC COOPERATIVITY OF LIGAND-RESPONSIVE REG- ULATOR TRAP VIA STATISTICAL THERMODYNAMIC MODELING AND PROTEIN POS486 ENGINEERING PROBING FUNCTIONAL PROTEIN DYNAMICS THROUGH NATIVE-STATE HY- Weicheng Li (1), Elihu Ihms, Ian Kleckner, Melody Holmquist, Vicki Wysocki, DROGEN EXCHANGE MASS SPECTROMETRY Paul Gollnick, Mark Foster Kimberly Burnett (1), Max Paul, Katie Ventre, Sheila Jaswal (1) The Ohio State Univerisity (Columbus, United States) (1) Amherst College Biochemistry & Biophysics Program (Amherst, United States) POS494 POS487 PROBING THE MULTIFACETED ROLE OF MAGNESIUM ON INTEGRIN-COLLA- A NEXT-GENERATION NAÏVE UBIQUITIN LIBRARY FOR THE DEVELOPMENT OF GEN RECOGNITION INTRACELLULAR AFFINITY REAGENTS Conceicao A.S.A. Minetti (1), Ana Monica Nunes, David P. Remeta, Jean Baum Kevin Davis (1), Sachdev Sidhu (1) Rutgers University (Piscataway, United States) (1) University of Toronto (Toronto, Canada) 156 157 #PS32 POS502 Posters TARGETING THE BECLIN 1 COILED COIL DOMAIN WITH STAPLED PEPTIDES TO ENHANCE AUTOPHAGY AND ENDOLYSOSOMAL TRAFFICKING POS495 Yanxiang Zhao (1), Shuai Wu, Yunjiao He, Xianxiu Qiu, Wenchao Yang RAF AND MEMBRANE MIMICS MODULATE RAS DIMERIZATION (1) The Hong Kong Polytechnic University (Hung Hom, China) Morgan Packer (1), Jillian Parker, Kendra Marcus, Jean Chung, Young Lee, Lee Makowski, Jay Groves, Carla Mattos POS503 (1) Department of Chemistry and Chemical Biology, Northeastern University RECONSTRUCTION OF AN ANCESTRAL LACI/GALR FAMILY TRANSCRIPTION (Boston, United States) FACTOR Matthew Spence (1), Joe Kaczmarski, Nobuhiko Tokuriki, Colin Jackson POS496 (1) Australian National University (Canberra, Australia) SINGLE MOLECULE DETECTION OF WEST NILE VIRUS NS2B-NS3 PROTEASE USING OMPG NANOPORE SENSOR POS504 Spencer Shorkey (1) PREDICTING PDZ-PEPTIDE BINDING STRENGTHS IN SILICO (1) University of Massachusetts Amherst (Amherst, United States) Katherine McCoy (1), Gevorg Grigoryan (1) Dartmouth College (White River Junction, United States) POS497 UNDERSTANDING THE KINETICS AND REGULATION OF GLUCAN PHOSPHATASES POS505 Tiffany Henao (1), Madushi Raththagala COMPUTATIONALLY PREDICTING DYNAMICS AND ALLOSTERY USING TERTIARY (1) Skidmore College (Saratoga Springs, United States) MOTIFS Jack Holland (1), Gevorg Grigoryan POS499 (1) Dartmouth College (Hanover, United States) COMPUTATIONAL DESIGN AND FUNCTIONALIZATION OF POROUS TWO-RING ALPHA-HELICAL BUNDLES POS510 Chunfu Xu (1), Peilong Lu, Xue Yuan Pe, Scott Boyken, Ben Luisi, David Baker MASS SPECTROMETRY BASED PROTEOMICS APPROACH TO IDENTIFY BIO- (1) University of Washington (Seattle, United States) MARKERS FOR THE DIAGNOSIS AND TREATMENT OF OBSTRUCTIVE SLEEP APNEA POS500 Cristiana Dumbrăveanu (1) STUDYING THE EFFECTS OF A SMALL MOLECULE INHIBITOR ON A RAS-RELAT- (1) Clarkson University ( Potsdam, United States) ED PROTEIN Djamali Muhoza (1), Paul Adams POS511 (1) University of Arkansas (Fayetteville, United States) POSTEVOLUTIONARY GENETIC VARIATION, 3D STRUCTURE AND DESIGN Debora Marks (1), Systems Biology POS501 (1) Harvard Medical School IN SILICO STRUCTURAL ANALYSIS OF ELONGATION FACTOR-1 ALPHA AND ELONGATION FACTOR-LIKE Kotaro Sakamoto (1), Megumi Kayanuma, Yasuteru Shigeta (1) Center for Computational Sciences, University of Tsukuba (Tsukuba, Japan)

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33rd Annual Symposium June 30 - July 3, 2019

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