DOCSLIB.ORG

Reversible Assembly and Amyloidogenesis of The

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Reversible Assembly and Amyloidogenesis of The Reversible assembly and amyloidogenesis of the staphylococcal biofilm protein, Aap A dissertation submitted to the Graduate School of the University of Cincinnati In partial fulfillment of the requirements for the degree of Doctor of Philosophy In the Department of Molecular Genetics, Biochemistry and Microbiology of the College of Medicine 2019 Alexander E. Yarawsky B.S. Biological Sciences and Chemistry Northern Kentucky University 2013 Committee Chair: Andrew B. Herr, Ph.D. Abstract The human skin commensal, Staphylococcus epidermidis, is the bacterium most commonly responsible for hospital-acquired infections. This microbe has a very strong capacity for forming bacterial communities known as biofilms. These communities are well-structured and often involve a slime-like matrix of extracellular polysaccharide which assists in bacterial accumulation. A well-known protein factor, the accumulation- associated protein (Aap), can also mediate intercellular adhesion, contributing the biofilm formation. Interestingly, Aap has been shown to be critical for infection in a rat catheter model, whereas the extracellular polysaccharide was irrelevant in infection. Aap is a large, multi-functional, cell wall-anchored protein expressed by S. epidermidis. The N-terminus of the protein contains a region of short repeats called the A-repeats, followed by a globular lectin domain. The lectin domain can mediate attachment of bacteria to a surface. A proteolytic cleavage site downstream of the lectin domain leads to the release of the A-repeats and lectin domain, allowing Aap to function in accumulation. There are 5 - 17 B-repeats downstream of the cleavage site, which can assembly with Aap on adjacent cells in the presence of Zn2+. At the C-terminus of Aap lies a region of low complexity, which is rich in proline and glycine residues. After this region is a cell wall-anchoring motif that results in the covalent attachment of Aap to the bacterial cell wall. Much of the progress made toward understanding the structure and biological function of the B-repeats has utilized a minimal construct containing one and a half B- repeats (Brpt1.5). Previous members of the Herr Lab have determined that Brpt1.5 can ii assemble into an anti-parallel dimer in the presence of Zn2+. Interestingly, while the Brpt1.5 dimer would disassociate in the presence of Zn2+-chelator, mature biofilms were unaffected by addition of the chelator. This led members of the Herr Lab to express and characterize longer B-repeat constructs, which more closely resemble the number of B- repeats observed in Aap and show Zn2+-dependent assembly beyond dimer, eventually forming amyloid-like fibers. Amyloid fibers are often associated with toxicity, however, the fibers formed by Aap's B-repeats are utilized by the bacterium in a functionally beneficial way. In several other bacteria, functional amyloids have been shown to provide added strength to the biofilm structure. In the work presented here, we show Aap forms fibers in S. epidermidis biofilms and are responsible for the biofilm's resistance toward Zn2+-chelator. We also characterize a recently discovered protein, small basic protein (Sbp), which is able to reduce the amount of Zn2+ required for B- repeat aggregation. We propose that Sbp is a nucleating or accessory protein for Aap- amyloidogenesis. Finally, a secondary interest of this dissertation work is to characterize the structure of the proline/glycine-rich stalk-like region of Aap and other cell wall-anchored proteins. Interestingly, several of these regions have a very high propensity to remain extended in solution, primarily due to the high polyproline type II helix propensity. Overall, this dissertation work has led to an increased understanding of the mechanism of Aap-dependent accumulation in biofilm formation. iii iv Acknowledgements I would like to thank my advisor, Dr. Andrew Herr for always being enthusiastic about my data and inspiring me to continue down the path of biophysics. I thank my fellow lab members for constant discussions about various aspects of my research, as well as for entertaining outings. I also owe the previous lab members who had set the stage for my projects, especially Deb Conrady and Stefanie Johns. I would also like to thank my undergraduate advisor at Northern Kentucky University, Dr. Heather Bullen, for showing me the excitement of research and being an inspirational mentor. I am grateful for my many trips to the Gibbs Conference on Biological Thermodynamics, which are always inspiring me to maintain a high degree of rigor in my work, and have led to me reading many papers from the influential biophysicists that are or once were associated with this meeting. I would like to thank Beckman Coulter for awarding me a full travel grant to attend the 23rd International Analytical Ultracentrifugation Workshop and Symposium (AUC 2017) where I learned a great deal from many experts in the field, particularly in regards to Walter Stafford's SEDANAL software. I must acknowledge my family and friends as well, especially my wife Danille, who have supported my journey and who have encouraged me to pursue the highest of goals. v Table of Contents Title Page ........................................................................................................................ i Abstract .......................................................................................................................... ii Acknowledgements ....................................................................................................... v Table of Contents ......................................................................................................... vi List of Figures and Tables ............................................................................................ x Chapter I. Literature Review ......................................................................................... 1 A. The importance of staphylococcal biofilms in the healthcare industry ..................... 1 B. Molecular pathways of staphylococcal biofilm formation ......................................... 2 i. Steps of biofilm formation ...................................................................................... 3 ii. PNAG-dependent accumulation ............................................................................ 8 iii. Protein-dependent accumulation ........................................................................ 10 C. The accumulation-associated protein .................................................................... 13 i. Aap domain architecture ...................................................................................... 14 ii. Role of Aap in attachment ................................................................................... 14 iii. Zn2+-mediated self-assembly of Aap (role in accumulation) ............................... 17 D. Considerations in Protein Folding and Stability ..................................................... 21 i. The hydrophobic effect ........................................................................................ 22 ii. Solvent-solute interactions .................................................................................. 23 iii. Solute-solute interactions ................................................................................... 27 E. Protein misfolding and natively unfolded proteins .................................................. 31 i. Protein aggregation and amyloid formation ......................................................... 31 a. Amyloid stability ............................................................................................... 32 b. Pathogenic vs. functional amyloid ................................................................... 33 ii. Intrinsically disordered proteins ........................................................................... 34 a. Factors determining conformational propensities ............................................ 34 b. Functional roles of IDPs .................................................................................. 36 F. Goals of dissertation work...................................................................................... 39 References ................................................................................................................. 42 Chapter II. The biofilm adhesion protein Aap from Staphylococcus epidermidis forms zinc-dependent amyloid fibers ........................................................................ 54 Abstract ...................................................................................................................... 55 Author Summary ........................................................................................................ 57 Introduction ................................................................................................................ 58 Solution characterization of tandem B-repeats from Aap ........................................... 62 Tandem B-repeats assemble into multiple higher-order species in the presence of Zn2+ ............................................................................................................................ 64 2D size-and-shape sedimentation analysis indicates formation of fiber-like species . 67 Tandem B-repeats form amyloid fibers in the presence of Zn2+ ................................. 71 vi B-repeat fiber assembly is time- and temperature-dependent ..................................
Load more

Recommended publications
  • Biographical Information
    Curriculum Vitae Sharon Hammes-Schiffer Department of Chemistry phone: (203) 432-3915 Yale University 225 Prospect Street e-mail: [email protected] New Haven, CT 06520-8107 http://hammes-schiffer-group.org/ Date of Birth May 27, 1966 Education B.A. Chemistry Princeton University 5/88 summa cum laude, Highest Honors in Chemistry Ph.D. Chemistry Stanford University 9/93 Graduate advisor: Hans C. Andersen Professional Experience John Gamble Kirkwood Professor of Chemistry 1/18 – present Yale University Swanlund Professor of Chemistry 8/12 − 12/17 University of Illinois at Urbana-Champaign Eberly Professor in Biotechnology 8/06 − 8/12 Pennsylvania State University Professor of Chemistry 7/03 − 8/12 Pennsylvania State University Shaffer Associate Professor of Chemistry 8/00 − 7/03 Pennsylvania State University Clare Boothe Luce Assistant Professor of Chemistry 8/95 − 8/00 University of Notre Dame Postdoctoral research scientist AT&T Bell Laboratories 9/93 − 8/95 AT&T Bell Laboratories, Murray Hill, NJ Postdoctoral supervisor: John C. Tully Honors and Awards G. M. Kosolapoff Award from Auburn University, 2019 Member, Connecticut Academy of Science and Engineering (CASE), 2018 Center for Advanced Study Professor, University of Illinois Urbana-Champaign, 2017 Senior Fellow, Canadian Institute for Advanced Research (CIFAR), 2016 − present Fellow, Biophysical Society, 2015 Blue Waters Professor, 2014 – 2018 Member, International Academy of Quantum Molecular Science, 2014 Member, U.S. National Academy of Sciences, 2013 Fellow, American Association for the Advancement of Science, 2013 Member, American Academy of Arts and Sciences, 2012 Fellow, American Chemical Society, 2011 National Institutes of Health MERIT Award, 2011 1 Sharon Hammes-Schiffer CV -- 08/27/18 Fellow, American Physical Society, 2010 American Chemical Society Akron Section Award, 2008 International Academy of Quantum Molecular Science Medal, 2005 Iota Sigma Pi Agnes Fay Morgan Research Award, 2005 Alexander M.
    [Show full text]
  • High-Pressure X-Ray Crystallography and Core Hydrophobicity of T4
    HIGH-PRESSURE X-RAY CRYSTALLOGRAPHY AND CORE HYDROPHOBICITY OF T4 LYSOZYMES A Dissertation Presented to the Faculty of the Graduate School of Cornell University in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy by Marcus David Collins January 2006 This document is in the public domain. HIGH-PRESSURE X-RAY CRYSTALLOGRAPHY AND CORE HYDROPHOBICITY OF T4 LYSOZYMES Marcus David Collins, Ph.D. Cornell University 2006 While a great many protein structures are now known, considerably less is known experimentally about how these molecules reversibly fold and unfold into nearly unique, active structures. For more than 50 years, the central hypothesis has been that micro-scale phase separation between oil-like non-polar and charged or po- lar amino acid residues drives the formation of a “hydrophobic” protein core. A great deal of evidence supports this hypothesis, but the unfolding of proteins as a response to pressure contradicts it. A possible solution is the suggestion that pres- sure induced unfolding is a different process from thermally or chemically driven unfolding. Separately, little is known about the structural response of proteins to pressure, although pressure has clear and sometimes large effects on protein activ- ity and stability. For these reasons, we have chosen to study the cavity-containing mutant L99A of T4 Lysozyme, along with the wild-type protein, under pressures up to 2 kbar, a compression of about 0.1%. The protein is remarkably incompress- ible, and the presence of a cavity has almost no impact on the pressure response over the wild-type lysozyme. Instead, four water molecules cooperatively fill the cavity, interacting with each other and the protein roughly equally.
    [Show full text]
  • 15/5/40 Liberal Arts and Sciences Chemistry Irwin C. Gunsalus Papers, 1877-1993 BIOGRAPHICAL NOTE Irwin C
    15/5/40 Liberal Arts and Sciences Chemistry Irwin C. Gunsalus Papers, 1877-1993 BIOGRAPHICAL NOTE Irwin C. Gunsalus 1912 Born in South Dakota, son of Irwin Clyde and Anna Shea Gunsalus 1935 B.S. in Bacteriology, Cornell University 1937 M.S. in Bacteriology, Cornell University 1940 Ph.D. in Bacteriology, Cornell University 1940-44 Assistant Professor of Bacteriology, Cornell University 1944-46 Associate Professor of Bacteriology, Cornell University 1946-47 Professor of Bacteriology, Cornell University 1947-50 Professor of Bacteriology, Indiana University 1949 John Simon Guggenheim Fellow 1950-55 Professor of Microbiology, University of Illinois 1955-82 Professor of Biochemistry, University of Illinois 1955-66 Head of Division of Biochemistry, University of Illinois 1959 John Simon Guggenheim Fellow 1959-60 Research sabbatical, Institut Edmund de Rothchild, Paris 1962 Patent granted for lipoic acid 1965- Member of National Academy of Sciences 1968 John Simon Guggenheim Fellow 1972-76 Member Levis Faculty Center Board of Directors 1977-78 Research sabbatical, Institut Edmund de Rothchild, Paris 1973-75 President of Levis Faculty Center Board of Directors 1978-81 Chairman of National Academy of Sciences, Section of Biochemistry 1982- Professor of Biochemistry, Emeritus, University of Illinois 1984 Honorary Doctorate, Indiana University 15/5/40 2 Box Contents List Box Contents Box Number Biographical and Personal Biographical Materials, 1967-1995 1 Personal Finances, 1961-65 1-2 Publications, Studies and Reports Journals and Reports, 1955-68
    [Show full text]
  • Center for History of Physics Newsletter, Spring 2008
    One Physics Ellipse, College Park, MD 20740-3843, CENTER FOR HISTORY OF PHYSICS NIELS BOHR LIBRARY & ARCHIVES Tel. 301-209-3165 Vol. XL, Number 1 Spring 2008 AAS Working Group Acts to Preserve Astronomical Heritage By Stephen McCluskey mong the physical sciences, astronomy has a long tradition A of constructing centers of teaching and research–in a word, observatories. The heritage of these centers survives in their physical structures and instruments; in the scientific data recorded in their observing logs, photographic plates, and instrumental records of various kinds; and more commonly in the published and unpublished records of astronomers and of the observatories at which they worked. These records have continuing value for both historical and scientific research. In January 2007 the American Astronomical Society (AAS) formed a working group to develop and disseminate procedures, criteria, and priorities for identifying, designating, and preserving structures, instruments, and records so that they will continue to be available for astronomical and historical research, for the teaching of astronomy, and for outreach to the general public. The scope of this charge is quite broad, encompassing astronomical structures ranging from archaeoastronomical sites to modern observatories; papers of individual astronomers, observatories and professional journals; observing records; and astronomical instruments themselves. Reflecting this wide scope, the members of the working group include historians of astronomy, practicing astronomers and observatory directors, and specialists Oak Ridge National Laboratory; Santa encounters tight security during in astronomical instruments, archives, and archaeology. a wartime visit to Oak Ridge. Many more images recently donated by the Digital Photo Archive, Department of Energy appear on page 13 and The first item on the working group’s agenda was to determine through out this newsletter.
    [Show full text]
  • B I O T E C H I N T H E S U N S H I N E S T A
    BIOTECH IN THE SUNSHINE STATE December 2009 American Society for Biochemistry and Molecular Biology ASBMB2011 SPECIAL SYMPOSIA CALL FOR PROPOSALS Partner with the American Society for Biochemistry and Molecular Biology to bring your community together! ASBMB Special Symposia provides you, as a specialized researcher, a unique opportunity to present cutting-edge science mixed with active networking opportunities in an intimate setting. How We’re Different: Format: Majority of talks selected from abstracts, invited speakers, 2-4 days in length Attendee: 60- 200 attendees, including investigators, industry professionals, graduate and postdoctoral students Venues: Unique locations near natural resources that enable time for outdoor recreation and networking opportunities Funding: ASBMB provides initial funding as well as staff support! Learn More About Special Symposia and Proposal Submission Guidelines at www.asbmb.org/meetings Proposals Due March 1, 2010 ATodayFullPageAd_2011_Proposal Submission2.indd 1 11/23/2009 10:50:10 AM contents DECEMBER 2009 On the cover: ASBMB hopes that your holidays are filled with society news lots of serotonin. 2 Letters to the Editor IMAGE: REBECCA HANNA 20 4 President’s Message 7 Washington Update 8 News from the Hill 11 Member Spotlight 12 Retrospective: Mahlon Hoagland (1921-2009) A retrospective 15 Retrospective: on Mahlon Charles Tanford (1921-2009) Hoagland. 12 2010 annual meeting 18 Nobel Laureate Claims the 2010 Herbert Tabor Lectureship 19 Kinase Researcher Named Recipient of FASEB Award special interest 20 Centerpieces: Burnham Institute Touches Down in Orlando departments 26 Education and Training Regulating 30 Minority Affairs transcriptional activity. 32 BioBits 32 34 Career Insights 36 Lipid News resources Scientific Meeting Calendar podcast summary online only Check out the latest ASBMB podcast, in which Journal of Biological Chemistry Associate Editor James N.
    [Show full text]
  • The Hydrodynamic and Conformational Properties of Denatured Proteins in Dilute Solutions
    The hydrodynamic and conformational properties of denatured proteins in dilute solutions Guy C. Berry* Department of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213 Received 13 August 2009; Accepted 3 November 2009 DOI: 10.1002/pro.286 Published online 13 November 2009 proteinscience.org Abstract: Published data on the characterization of unfolded proteins in dilute solutions in aqueous guanidine hydrochloride are analyzed to show that the data are not fit by either the random flight or wormlike chain models for linear chains. The analysis includes data on the intrinsic viscosity, root-mean-square radius of gyration, from small-angle X-ray scattering, and hydrodynamic radius, from the translational diffusion coefficient. It is concluded that residual structure consistent with that deduced from nuclear magnetic resonance on these solutions can explain the dilute solution results in a consistent manner through the presence of ring structures, which otherwise have an essentially flexible coil conformation. The ring structures could be in a state of continual flux and rearrangement. Calculation of the radius of gyration for the random- flight model gives a similar reduction of this measure for chains joined at their endpoints, or those containing loop with two dangling ends, each one-fourth the total length of the chain. This relative insensitivity to the details of the ring structure is taken to support the behavior observed across a range of proteins. Keywords: protein; radius of gyration; intrinsic viscosity; loop formation Introduction analysis, with such studies often motivated by inter- In a 2005 article devoted to the discussion of ‘‘the est in the folding of the denatured chain.
    [Show full text]
  • Charles Phelps Smyth 1895–1990
    NATIONAL ACADEMY OF SCIENCES CHARLES PHELPS SMYTH 1 8 9 5 – 1 9 9 0 A Biographical Memoir by BY WALTER KAUZMANN AND JOHN D. ROB ERTS Any opinions expressed in this memoir are those of the authors and do not necessarily reflect the views of the National Academy of Sciences. Biographical Memoir COPYRIGHT 2010 NATIONAL ACADEMY OF SCIENCES WASHINGTON, D.C. CHARLES PHELPS SMYTH February 10, 1895–March 18, 1990 BY WALTER KAUZMANN AND JOHN D . RO B ERTS HARLES PHELPS SMYTH WAS BORN ON FEBRUARY 10, 1895, in CClinton, New York, where his father, Charles Henry Smyth, was a professor of geology and mineralogy at Hamilton College. Princeton President Woodrow Wilson called Charles Henry to Princeton University in 1905. He served on the faculty as a professor of geology until his retirement in 194 and played an important role in building Princeton’s graduate program in geology. At the age of 10 Charles Phelps with his younger brother, Henry D., moved to Princeton. Here the members of the Smyth family—father, mother, and sons—lived out most of their remaining lives. Charlie attended Miss Fine’s School and Lawrenceville before entering Princeton University in the class of 1916. He graduated in chemistry with highest honors (he had been among the first group of students to be admitted to Phi Beta Kappa as juniors), and then stayed on for a year, receiving an M.A. in 1917. During World War I, he served in Washington, first with the Bureau of Standards, then as a first lieutenant in the Chemical Warfare Service.
    [Show full text]
  • Proceedings of the American Philosophical Society Vol. 120, Num
    Proceedings of the American Philosophical Society Vol. 120, Num. 1. Año 1976 Held at Philadelphia for Promoting Useful Knowledge Fred L. Whipple. “Comet Kohoutek in Retrospect” Proceedings of the American Philosophical Society. Vol. 120, Num. 1. Año 1976; pagina 1-6 Myron P. Gilmore. “The Berensons and Villa I Tatti” Proceedings of the American Philosophical Society. Vol. 120, Num. 1. Año 1976; pagina 7-12 Helen B. Taussig. “The Development of the Blalock-Taussing Operation and Its Results Twenty Years Later” Proceedings of the American Philosophical Society. Vol. 120, Num. 1. Año 1976; pagina 13-20 Ward H. Goodenough. “On the Origin of Matrilineal Clans: A “Just So” Story” Proceedings of the American Philosophical Society. Vol. 120, Num. 1. Año 1976; pagina 21-36 Leon N. Cooper. “How Possible Becomes Actual in the Quantum Theory” Proceedings of the American Philosophical Society. Vol. 120, Num. 1. Año 1976; pagina 37-45 John Owen King. “Labors of the Estranged Personality: Josiah Royce on “The Case of John Bunyan”” Proceedings of the American Philosophical Society. Vol. 120, Num. 1. Año 1976; pagina 46-58 Stanley A. Czarnik. “The Theory of the Mesolithic in European Archaeology” Proceedings of the American Philosophical Society. Vol. 120, Num. 1. Año 1976; pagina 59-66 Proceedings of the American Philosophical Society Vol. 120, Num. 2. Año 1976 Held at Philadelphia for Promoting Useful Knowledge Jonathan E. Rhoads. “New Approaches in the Study of Neoplasia: Preliminary Remarks for the Symposium” Proceedings of the American Philosophical Society. Vol. 120, Num. 2. Año 1976; pagina 67-68 Sol Spiegelman. “The Search for Viruses in Human Cancer” Proceedings of the American Philosophical Society.
    [Show full text]
  • Dr. Kokichi Hanaoka, Ph.D
    The Discovery of the Enhanced Property of Water Supporting Life and Ecology Final Version – Not for Distribution Authored By: Kokichi Hanaoka Ph.D. 1 Table of Contents 2 Introduction 5 Chapter 1 A Functional Water Supporting Life’s Activities 8 Water which creates life and sustains the human body 9 Water that satisfies each cell 9 Water which circulates and works inside and outside of cells 11 Discovery of the water channel - aquaporin 13 Characteristics of heat and cold in support of life 14 A dryness of the throat is a warning signal 16 Cautions on the quantity and quality of water replenishment 17 Chapter 2 Where does this power of water come from? 19 One drop of water with an infinite number of water molecules 20 Birth of hydrogen that composes water 21 Different elements resulting from hydrogen 22 Oxygen bonds with hydrogen to produce water 23 Imagine the shape of a water molecule 24 Hydrogen bond that becomes the source of power 26 Hydrogen bond that brings out the mystique of water 27 Water molecules that move like a dancing spectacle 29 Reasons why water dissolves matter 30 Non-freezable water and proteins 31 From philosophy of water to science 33 A surprising property where liquid is heavier than a solid 34 Creating a relaxing environment 36 Various kinds of water on earth 37 Chapter 3 Water inside the body 38 Traces of life that were born in the sea 39 Mystery of non-freezable water inside the cell 40 The power of water inside the DNA structure 41 Wonder of water that changes itself to synchronize with the environment 42 Mineral
    [Show full text]
  • Glasses and the Historical Research
    Glasses and the historical research Jaroslav Sestak DISTINCTIVE ANNIVERSARIES, PAPERS AND CITATION RECORDS IN THE TOPIC OF GLASS CRYSTALLIZATION Sklář a keramik 11–12 / 2011 – 265 F R E D E R I K WILIE. H. Z A C H A R I A S E N BIBLIOGRAPHY IN MEMORIAM: WALTER KAUZMANN (1916–2009) C.A. Angell, D.R.McFarlane and M. Oguni KAUZMANN PARADOX, METASBLE LIQUIDS AND IDEAL GLASSES Annals of N.Y. Academy of Sciences David Turnbull UNDER WHAT CONDITIONS CAN A GLASS BE FORMED? Contemp. Phys., 1969, VOL. 10, NO. 5, 473-488 Jaroslav Šesták GLASSES AND ITS HISTORY Assay Některá výročí, publikace a citovanost v oboru krystalizace skel Distinctive anniversaries, papers and citation records in the topic of glass crystallization Jaroslav Šesták Nové technologie – Výzkumné centrum západočeského regionu, Západočeská universita, Universitní 8, CZ-30114 Plzeň, E-mail: [email protected]; Sekce fyziky pevných látek, Fyzikální ústav AV ČR, v.v.i., Cukrovarnická 10, CZ-16200 Praha; E-mail: [email protected] Práce zveřejňuje osmnáct většinou neznámých fotografií vý- Eighteen unfamiliar photos of distinguished specialists in glass značných odborníků v oblasti studia fázových transformací skel research are exposed describing also their scientific contribu- a ukazuje jejich badatelský význam. Je též otištěna fotografie tions. The work of CT7 (of ICG-International Commission on pracovní skupiny CT7 (ICG-International Commission on Glass) Glass) is mentioned including its photo from the year 2000.. dlouhodobě pracující v oblasti krystalizace skel. Text zahrnuje Text shows the survey of recently published books and reveals přehled nedávno publikovaných knih a analyzuje citační odezvy the best cited papers published in selected journals dealing with nejcitovanější publikací (podle WOS), zejména v časopisech Czech the topic of glass crystallization such as Czech J Phys, J Thermal J Phys, J Thermal Anal, Thermochim Acta, J Nocryst Sol, Phys Anal, Thermochim Acta, J Nonocryst Solids, Phys Chem Glasses, Chem Glasses, J Amer Cer Soc a Silikáty.
    [Show full text]
  • HENRY EYRING February 20, 1901–December 26, 1981
    NATIONAL ACADEMY OF SCIENCES H E N R Y E YRIN G 1901—1981 A Biographical Memoir by W A L T E R KAUZMANN Any opinions expressed in this memoir are those of the author(s) and do not necessarily reflect the views of the National Academy of Sciences. Biographical Memoir COPYRIGHT 1996 NATIONAL ACADEMIES PRESS WASHINGTON D.C. Courtesy of the University of Utah HENRY EYRING February 20, 1901–December 26, 1981 BY WALTER KAUZMANN ENRY EYRING WAS FORTUNATE in entering the arena of chem- Hical physics at the time that quantum mechanics be- gan impinging on the fundamental problems of chemistry. He was also fortunate in possessing to an unusual degree a fertile imagination, unbounded curiosity, a warm and out- going personality, a high degree of intellectual talent, the ability to work hard, and a determination to succeed. The result was that, beginning in the early years of the 1930s, he exerted an important influence on the large numbers of students and colleagues lucky enough to come into contact with him. This influence continued to spread throughout the chemical community for the rest of his life. He broke new ground in a wide sweep of scientific activi- ties, involving matters that ranged from fundamental prin- ciples of chemistry to problems of a highly practical and applied nature. Some of his ideas contain elements that remain controversial and a considerable number of con- temporary scientists continue to work on them. Eyring was born in 1901 in the prosperous Mormon com- munity of Colonia Juarez, Mexico (about 100 miles south of Columbus, New Mexico).
    [Show full text]
  • Curriculum Vitae
    CURRICULUM VITAE William Esco (W. E.) Moerner Harry S. Mosher Professor and Professor, by courtesy, of Applied Physics Department of Chemistry and Biophysics Program Stanford University, Stanford, California 94305-5080 650-723-1727 (phone), 650-725-0259 (fax), e-mail: [email protected] Education 1975 B.S. Physics Washington University (Final Honors) St. Louis, Missouri B.S. Electrical Engineering (Final Honors) A.B. Mathematics (summa cum laude) 1978 M.S. Cornell University (Physics) Ithaca, New York 1982 Ph.D. Cornell University (Physics) Ithaca, New York Thesis Topic: Vibrational Relaxation Dynamics of an IR-Laser-Excited Molecular Impurity Mode in Alkali Halide Lattices Thesis Advisor: Professor A. J. Sievers Academic Honors 1963-82 Grade Point Average of All A's (4.0) 1971-75 Alexander S. Langsdorf Engineering Fellow, Washington University 1975 Dean's Award for Unusually Exceptional Academic Achievement 1975 Ethan A. H. Shepley Award for Outstanding Achievement (university-wide) 1975-79 National Science Foundation Graduate Fellow Career Summary 2016- Affiliated Faculty Member, Stanford Neurosciences Institute 2014- Faculty Fellow, ChEM-H at Stanford 2011-2014 Chemistry Department Chair 2005- Professor, by courtesy, of Applied Physics 2002- Harry S. Mosher Professor of Chemistry 1998- Professor of Chemistry Department of Chemistry Stanford University 1 Multidisciplinary education and research program on single-molecule spectroscopy, imaging, and quantum optics in solids, proteins, and liquids; single-molecule biophysics in cells;
    [Show full text]