Crystallization and Preliminary X-Ray Diffraction Analysis of P450terp And
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The Evolution of Hemoglobin. by Ross Hardison
American Scientist March-April 1999 v87 i2 p126(1) Page 1 the evolution of hemoglobin. by Ross Hardison A comparative study of hemoglobin was conducted to explain how an ancestral single-function molecule gave rise to descending molecules with varied functions. Hemoglobin is the molecule in red blood cells responsible for giving blood its color and for carrying oxygen throughout the body. New functions of metallo-porphyrin rings or a kind of molecular cage embedded in proteins were developed with the appearance of atmospheric oxygen. The presence of hemoglobin in both oxygen-needing and non-oxygen needing organisms suggests the same evolutionary roots. © COPYRIGHT 1999 Sigma Xi, The Scientific Research If similar compounds are used in all of these reactions, Society then how do the different functions arise? The answer lies in the specific structure of the organic component, most Studies of a very ancient protein suggest that changes in often a protein, that houses the porphyrin ring. The gene regulation are an important part of the evolutionary configuration of each protein determines what biochemical story service the protein will perform. The appearance of atmospheric oxygen on earth between Because they have such an ancient lineage, the one and two billion years ago was a dramatic and, for the porphyrin-containing molecules provide scientists with a primitive single-celled creatures then living on earth, a rare opportunity to follow the creation of new biological potentially traumatic event. On the one hand, oxygen was compounds from existing ones. That is, how does an toxic. On the other hand, oxygen presented opportunities ancestral molecule with a single function give rise to to improve the process of metabolism, increasing the descendant molecules with varied functions? In my efficiency of life’s energy-generating systems. -
Bottom-Up Self-Assembly Based on DNA Nanotechnology
nanomaterials Review Bottom-Up Self-Assembly Based on DNA Nanotechnology 1, 1, 1 1 1,2,3, Xuehui Yan y, Shujing Huang y, Yong Wang , Yuanyuan Tang and Ye Tian * 1 College of Engineering and Applied Sciences, State Key Laboratory of Analytical Chemistry for Life Science, Nanjing University, Nanjing 210023, China; [email protected] (X.Y.); [email protected] (S.H.); [email protected] (Y.W.); [email protected] (Y.T.) 2 Shenzhen Research Institute of Nanjing University, Shenzhen 518000, China 3 Chemistry and Biomedicine Innovation Center, Nanjing University, Nanjing 210023, China * Correspondence: [email protected] These authors contributed equally to this work. y Received: 9 September 2020; Accepted: 12 October 2020; Published: 16 October 2020 Abstract: Manipulating materials at the atomic scale is one of the goals of the development of chemistry and materials science, as it provides the possibility to customize material properties; however, it still remains a huge challenge. Using DNA self-assembly, materials can be controlled at the nano scale to achieve atomic- or nano-scaled fabrication. The programmability and addressability of DNA molecules can be applied to realize the self-assembly of materials from the bottom-up, which is called DNA nanotechnology. DNA nanotechnology does not focus on the biological functions of DNA molecules, but combines them into motifs, and then assembles these motifs to form ordered two-dimensional (2D) or three-dimensional (3D) lattices. These lattices can serve as general templates to regulate the assembly of guest materials. In this review, we introduce three typical DNA self-assembly strategies in this field and highlight the significant progress of each. -
Hemoglobin, Myoglobin and Neuroglobin in Endogenous Thiosulfate Production Processes
International Journal of Molecular Sciences Review The Role of Hemoproteins: Hemoglobin, Myoglobin and Neuroglobin in Endogenous Thiosulfate Production Processes Anna Bilska-Wilkosz *, Małgorzata Iciek, Magdalena Górny and Danuta Kowalczyk-Pachel Chair of Medical Biochemistry, Jagiellonian University Collegium Medicum ,7 Kopernika Street, Kraków 31-034, Poland; [email protected] (M.I.); [email protected] (M.G.); [email protected] (D.K.-P.) * Correspondence: [email protected]; Tel.: +48-12-4227-400; Fax: +48-12-4223-272 Received: 5 May 2017; Accepted: 16 June 2017; Published: 20 June 2017 Abstract: Thiosulfate formation and biodegradation processes link aerobic and anaerobic metabolism of cysteine. In these reactions, sulfite formed from thiosulfate is oxidized to sulfate while hydrogen sulfide is transformed into thiosulfate. These processes occurring mostly in mitochondria are described as a canonical hydrogen sulfide oxidation pathway. In this review, we discuss the current state of knowledge on the interactions between hydrogen sulfide and hemoglobin, myoglobin and neuroglobin and postulate that thiosulfate is a metabolically important product of this processes. Hydrogen sulfide oxidation by ferric hemoglobin, myoglobin and neuroglobin has been defined as a non-canonical hydrogen sulfide oxidation pathway. Until recently, it appeared that the goal of thiosulfate production was to delay irreversible oxidation of hydrogen sulfide to sulfate excreted in urine; while thiosulfate itself was only an intermediate, transient metabolite on the hydrogen sulfide oxidation pathway. In the light of data presented in this paper, it seems that thiosulfate is a molecule that plays a prominent role in the human body. Thus, we hope that all these findings will encourage further studies on the role of hemoproteins in the formation of this undoubtedly fascinating molecule and on the mechanisms responsible for its biological activity in the human body. -
Optimal Operation of an Integrated Bioreaction–Crystallization Process
中国科技论文在线 http://www.paper.edu.cn Chemical Engineering Science 56 (2001) 6165–6170 www.elsevier.com/locate/ces Optimal operation ofan integrated bioreaction–crystallization process for continuous production of calcium gluconate using external loop airlift columns Jie Baoa, Kenichi Koumatsua, Keiji Furumotob, Makoto Yoshimotoa, Kimitoshi Fukunagaa, Katsumi Nakaoa; ∗ aDepartment of Applied Chemistry and Chemical Engineering, Yamaguchi University, Tokiwadai, Ube, Yamaguchi 755-8611, Japan bOshima National College of Maritime Technology, Oshima, Yamaguchi 742-2106, Japan Abstract A kinetic model was proposed to optimize the integrated bioreaction–crystallization process newly developed for production of calcium gluconate crystals using external loop airlift columns. The optimal operating conditions in the bioreactor were determined using an objective function deÿned to maximize the productivity as well as to minimize biocatalyst loss. The optimization of the crystallizer was carried out by matching the crystallization rate to the optimal production rate in the bioreactor because the bioreaction was found to be the rate controlling process. The calcium gluconate productivity under the optimal conditions of the integrated process was obtained by the simulation based on the process model. The productivity ofthe proposed process was found to be comparable to that ofthe current batch fermentationprocess. ? 2001 Elsevier Science Ltd. All rights reserved. Keywords: Process kinetic model; Optimization; Calcium gluconate; Bioreaction–crystallization -
Adult, Embryonic and Fetal Hemoglobin Are Expressed in Human Glioblastoma Cells
514 INTERNATIONAL JOURNAL OF ONCOLOGY 44: 514-520, 2014 Adult, embryonic and fetal hemoglobin are expressed in human glioblastoma cells MARWAN EMARA1,2, A. ROBERT TURNER1 and JOAN ALLALUNIS-TURNER1 1Department of Oncology, University of Alberta and Alberta Health Services, Cross Cancer Institute, Edmonton, AB T6G 1Z2, Canada; 2Center for Aging and Associated Diseases, Zewail City of Science and Technology, Cairo, Egypt Received September 7, 2013; Accepted October 7, 2013 DOI: 10.3892/ijo.2013.2186 Abstract. Hemoglobin is a hemoprotein, produced mainly in Introduction erythrocytes circulating in the blood. However, non-erythroid hemoglobins have been previously reported in other cell Globins are hemo-containing proteins, have the ability to types including human and rodent neurons of embryonic bind gaseous ligands [oxygen (O2), nitric oxide (NO) and and adult brain, but not astrocytes and oligodendrocytes. carbon monoxide (CO)] reversibly. They have been described Human glioblastoma multiforme (GBM) is the most aggres- in prokaryotes, fungi, plants and animals with an enormous sive tumor among gliomas. However, despite extensive basic diversity of structure and function (1). To date, hemoglobin, and clinical research studies on GBM cells, little is known myoglobin, neuroglobin (Ngb) and cytoglobin (Cygb) repre- about glial defence mechanisms that allow these cells to sent the vertebrate globin family with distinct function and survive and resist various types of treatment. We have tissue distributions (2). During ontogeny, developing erythro- shown previously that the newest members of vertebrate blasts sequentially express embryonic {[Gower 1 (ζ2ε2), globin family, neuroglobin (Ngb) and cytoglobin (Cygb), are Gower 2 (α2ε2), and Portland 1 (ζ2γ2)] to fetal [Hb F(α2γ2)] expressed in human GBM cells. -
The Effects of Temperature on Hemoglobin in Capitella Teleta
THE EFFECTS OF TEMPERATURE ON HEMOGLOBIN IN CAPITELLA TELETA by Alexander M. Barclay A thesis submitted to the Faculty of the University of Delaware in partial fulfillment of the requirements for the degree of Master of Science in Marine Studies Summer 2013 c 2013 Alexander M. Barclay All Rights Reserved THE EFFECTS OF TEMPERATURE ON HEMOGLOBIN IN CAPITELLA TELETA by Alexander M. Barclay Approved: Adam G. Marsh, Ph.D. Professor in charge of thesis on behalf of the Advisory Committee Approved: Mark A. Moline, Ph.D. Director of the School of Marine Science and Policy Approved: Nancy M. Targett, Ph.D. Dean of the College of Earth, Ocean, and Environment Approved: James G. Richards, Ph.D. Vice Provost for Graduate and Professional Education ACKNOWLEDGMENTS I extend my sincere gratitude to the individuals that either contributed to the execution of my thesis project or to my experience here at the University of Delaware. I would like to give special thanks to my adviser, Adam Marsh, who afforded me an opportunity that exceeded all of my prior expectations. Adam will say that I worked very independently and did not require much guidance, but he served as an inspiration and a role model for me during my studies. Adam sincerely cares for each of his students and takes the time and thought to tailor his research program to fit each person's interests. The reason that I initially chose to work in Adam's lab was that he expressed a genuine excitement for science and for his lifes work. His enthusiasm resonated with me and helped me to find my own exciting path in science. -
Crystallization in Patterns: a Bio-Inspired Approach**
PROGRESS REPORTS Crystallization in Patterns: A Bio-Inspired Approach** By Joanna Aizenberg* Nature produces a wide variety of exquisite, highly functional mineralized tissues using simple inorganic salts. Biomineralization occurs within specific microenvironments, and is finely tuned by cells and specialized biomacromolecules. This article surveys bio- inspired approaches to artificial crystallization based on the above concept: that is, the use of organized organic surfaces patterned with specific initiation domains on a sub- micrometer scale to control patterned crystal growth. Specially tailored self-assembled monolayers (SAMs) of x-terminated alkanethiols were micropatterned on metal films using soft lithography and applied as organic templates for the nucleation of calcium carbonate. Crystallization results in the formation of large-area, high-resolution inorganic replicas of the underlying organic patterns. SAMs provide sites for ordered nucleation, and make it possible to control various aspects of the crystallization process, including the precise localization of particles, nucleation density, crystal sizes, crystallographic orientation, morphology, polymorph, stability, and architecture. The ability to construct periodic arrays of uniform oriented single crystals, large single crystals with controlled microporosity, or films presenting patterns of crystals offers a potent methodology to materials engineering. 1. Technological Challenge and Biological Of the many challenges facing materials science, the devel- Inspiration opment of an alternative, bottom±up crystallization route, which would enable the direct, patterned growth of crystals The ability to control crystallization is a critical requirement with controlled physico-chemical properties, became an at- in the synthesis of many technologically important materi- tractive, strategic goal. The fundamental principles of the [12±17] als.[1±5] Crystalline inorganic structures with micrometer-scale bottom±up approach can be borrowed from nature. -
Unsolved Problems in Nanotechnology
Unsolved Problems in Nanotechnology 61 Biographical sketch of Matthew Tirrell Matthew Tirrell received his undergraduate education in Chemical Engineering at Northwestern University and his Ph.D. in 1977 in Polymer Science from the University of Massachusetts. He is currently Dean of the College of Engineering at the University of California, Santa Barbara. From 1977 to 1999 he was on the faculty of Chemical Engineering and Materials Science at the University of Minnesota, where he served as head of the department from 1995 to 1999. His research has been in polymer surface properties including adsorption, adhesion, surface treatment, friction, lubrication and biocompatibilty. He has co-authored about 250 papers and one book and has supervised about 60 Ph.D. students. Professor Tirrell has been a Sloan and a Guggenheim Fellow, a recipient of the Camille and Henry Dreyfus Teacher-Scholar Award and has received the Allan P. Colburn, Charles Stine and the Professional Progress Awards from AIChE. He was elected to the National Academy of Engineering in 1997, became a Fellow of the American Institute of Medical and Biological Engineers in 1998, was elected Fellow of the American Association for the Advancement of Science in 2000 and was named Institute Lecturer for the American Institute of Chemical Engineers in 2001. 62 Unsolved Problems in Nanotechnology: Chemical Processing by Self-Assembly Matthew Tirrell Departments of Chemical Engineering and Materials Materials Research Laboratory California NanoSystems Institute University of California, Santa Barbara, CA 93106-5130 [email protected] Abstract The many impressive laboratory demonstrations of controllable self-assembly methods generate considerable hope and interest in self-assembly as a manufacturing method for nano-structured products. -
The Bio Revolution: Innovations Transforming and Our Societies, Economies, Lives
The Bio Revolution: Innovations transforming economies, societies, and our lives economies, societies, our and transforming Innovations Revolution: Bio The The Bio Revolution Innovations transforming economies, societies, and our lives May 2020 McKinsey Global Institute Since its founding in 1990, the McKinsey Global Institute (MGI) has sought to develop a deeper understanding of the evolving global economy. As the business and economics research arm of McKinsey & Company, MGI aims to help leaders in the commercial, public, and social sectors understand trends and forces shaping the global economy. MGI research combines the disciplines of economics and management, employing the analytical tools of economics with the insights of business leaders. Our “micro-to-macro” methodology examines microeconomic industry trends to better understand the broad macroeconomic forces affecting business strategy and public policy. MGI’s in-depth reports have covered more than 20 countries and 30 industries. Current research focuses on six themes: productivity and growth, natural resources, labor markets, the evolution of global financial markets, the economic impact of technology and innovation, and urbanization. Recent reports have assessed the digital economy, the impact of AI and automation on employment, physical climate risk, income inequal ity, the productivity puzzle, the economic benefits of tackling gender inequality, a new era of global competition, Chinese innovation, and digital and financial globalization. MGI is led by three McKinsey & Company senior partners: co-chairs James Manyika and Sven Smit, and director Jonathan Woetzel. Michael Chui, Susan Lund, Anu Madgavkar, Jan Mischke, Sree Ramaswamy, Jaana Remes, Jeongmin Seong, and Tilman Tacke are MGI partners, and Mekala Krishnan is an MGI senior fellow. -
Important Factors Influencing Protein Crystallization
Global Journal of Biotechnology and Biomaterial Science Mohnad Abdalla1*, Wafa Ali Eltayb1, Mini Review Abdus Samad1, Elshareef SHM1 and TIM Dafaalla2 1Hefei National Laboratory for Physical Sciences at the Important Factors Influencing Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People’s Protein Crystallization Republic of China 2College of Plant Science, Jilin University, Changchun 130062, China Abstract Dates: Received: 16 September, 2016; Accepted: The solution of crystallization problem was introduced around twenty years ago, with the 29 September, 2016; Published: 30 September, introduction of crystallization screening methods. Here reported some of the factors which affect 2016 protein crystallization, solubility, Concentration of precipitant, concentration of macromolecule, ionic *Corresponding author: Mohnad Abdalla, strength, pH, temperature, and organism source of macromolecules, reducing or oxidizing environment, Hefei National Laboratory for Physical Sciences additives, ligands, presence of substrates, inhibitors, coenzymes, metal ions and rate of equilibration. at the Microscale and School of Life Sciences, The aim of this paper to give very helpful advice for crystallization. University of Science and Technology of China, Hefei, Anhui 230027, PR China, E-mail: Buffer is most straight forward way to make a crystallization www.peertechz.com problem by effect the protein behave. There are many rules and Keywords: Proteins; Crystallization; Isoelectric point; different protein crystallization methods, some of it has been pH; Solubility; Stability developed during the recent years. However, Protein crystallization still represents a great challenge for bio crystallography. The Introduction cumulation of crystallization information in crystallization databases and in structural articles it allow us to design crystallization X-ray crystallography has provided 3D structures of thousands experiments depending on the character of the protein. -
Automated Protocols for Macromolecular Crystallization at the MRC Laboratory of Molecular Biology
Journal of Visualized Experiments www.jove.com Video Article Automated Protocols for Macromolecular Crystallization at the MRC Laboratory of Molecular Biology Fabrice Gorrec1, Jan Löwe1 1 Laboratory of Molecular Biology, Medical Research Council Correspondence to: Fabrice Gorrec at [email protected] URL: https://www.jove.com/video/55790 DOI: doi:10.3791/55790 Keywords: Biochemistry, Issue 131, X-ray crystallography, protein crystallization, high-throughput screening, fully automated system, nanoliter droplets, vapor diffusion, initial screen, nanoliter dispenser, liquid handler, crystal optimization, 4-corner method, additive screening Date Published: 1/24/2018 Citation: Gorrec, F., Löwe, J. Automated Protocols for Macromolecular Crystallization at the MRC Laboratory of Molecular Biology. J. Vis. Exp. (131), e55790, doi:10.3791/55790 (2018). Abstract When high quality crystals are obtained that diffract X-rays, the crystal structure may be solved at near atomic resolution. The conditions to crystallize proteins, DNAs, RNAs, and their complexes can however not be predicted. Employing a broad variety of conditions is a way to increase the yield of quality diffraction crystals. Two fully automated systems have been developed at the MRC Laboratory of Molecular Biology (Cambridge, England, MRC-LMB) that facilitate crystallization screening against 1,920 initial conditions by vapor diffusion in nanoliter droplets. Semi-automated protocols have also been developed to optimize conditions by changing the concentrations of reagents, the pH, or by introducing additives that potentially enhance properties of the resulting crystals. All the corresponding protocols will be described in detail and briefly discussed. Taken together, they enable convenient and highly efficient macromolecular crystallization in a multi-user facility, while giving the users control over key parameters of their experiments. -
Hemoprotein Dalam Tubuh Manusia Tinjauan Pustaka
http://jurnal.fk.unand.ac.id 22 Tinjauan Pustaka Hemoprotein dalam Tubuh Manusia Husnil Kadri Abstrak Hemoprotein adalah protein dengan kandungan hem yang terdapat hampir dalam semua sel manusia, hewan, dan pigmen fotosintesis tumbuhan. Ada berbagai macam hemoprotein yang tersebar luas dalam tubuh manusia, seperti hemoglobin, myoglobin, citoglobin, neuroglobin, dan lain-lain. Semua hemoprotein tersebut memiliki fungsi beragam yang penting untuk berlangsungnya proses metabolisme dalam tubuh. Struktur hem pada pigmen fotosintesis (klorofil) tumbuhan sama dengan hemoglobin pada manusia, tetapi ion logam pada klorofil adalah magnesium (Mg) sedangkan pada hemoglobin adalah besi (Fe). Perbedaan inilah yang kurang diketahui oleh sebagian masyarakat sehingga ada yang mengira mengkonsumsi klorofil tumbuhan dapat meningkatkan kadar hemoglobin darah. Oleh karena itu, artikel ini bertujuan untuk mengetahui perbedaan antara hemoprotein manusia dengan klorofil dan fungsi hemoprotein dalam tubuh manusia. Berdasarkan bentuk ion Fe pada gugus hemnya, maka hemoprotein dapat dibagi atas: (1) Hemoprotein yang memiliki ion Fe2+ sehingga mampu mengikat oksigen yaitu; hemoglobin, myoglobin, neuroglobin, dan cytoglobin. (2) Hemoprotein yang memiliki ion Fe3+ sehingga berperan sebagai enzim oksidoreduktase yaitu; Sitokrom P450, Sitokrom yang terlibat dalam fosforilasi oksidatif, katalase, triptopan pirolase, dan NO sintase. Kata kunci: hemoprotein, ion Fe2+, ion Fe3+ Abstract Hemoproteins are proteins containing heme that widely distributed in humans, animals, and photosynthetic pigment of plants. There are many kind of hemoproteins in human body, such as hemoglobin, myoglobin, cytoglobin, neuroglobin, etc. Hemoproteins have the varied functions to keep normal metabolism in the body. Photosynthetic pigment of plants (chlorophyll) and human’s hemoglobin have the same structure but the metal ions are different. Chlorophyll has magnesium and human’s hemoglobin has iron (Fe).