Investigating Native State Protein Dynamics Through Simulations Of Hydrogen Exchange Mass Spectrometry
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Author | : David D. Weis |
Publisher | : John Wiley & Sons |
Total Pages | : 422 |
Release | : 2016-03-21 |
Genre | : Science |
ISBN | : 1118616499 |
Hydrogen exchange mass spectrometry is widely recognized for its ability to probe the structure and dynamics of proteins. The application of this technique is becoming widespread due to its versatility for providing structural information about challenging biological macromolecules such as antibodies, flexible proteins and glycoproteins. Although the technique has been around for 25 years, this is the first definitive book devoted entirely to the topic. Hydrogen Exchange Mass Spectrometry of Proteins: Fundamentals, Methods and Applications brings into one comprehensive volume the theory, instrumentation and applications of Hydrogen Exchange Mass Spectrometry (HX-MS) - a technique relevant to bioanalytical chemistry, protein science and pharmaceuticals. The book provides a solid foundation in the basics of the technique and data interpretation to inform readers of current research in the method, and provides illustrative examples of its use in bio- and pharmaceutical chemistry and biophysics In-depth chapters on the fundamental theory of hydrogen exchange, and tutorial chapters on measurement and data analysis provide the essential background for those ready to adopt HX-MS. Expert users may advance their current understanding through chapters on methods including membrane protein analysis, alternative proteases, millisecond hydrogen exchange, top-down mass spectrometry, histidine exchange and method validation. All readers can explore the diversity of HX-MS applications in areas such as ligand binding, membrane proteins, drug discovery, therapeutic protein formulation, biocomparability, and intrinsically disordered proteins.
Author | : Yawen Bai |
Publisher | : Springer Science & Business Media |
Total Pages | : 332 |
Release | : 2008-02-04 |
Genre | : Science |
ISBN | : 1597451894 |
Covering experiment and theory, bioinformatics approaches, and state-of-the-art simulation protocols for better sampling of the conformational space, this volume describes a broad range of techniques to study, predict, and analyze the protein folding process. Protein Folding Protocols also provides sample approaches toward the prediction of protein structure starting from the amino acid sequence, in the absence of overall homologous sequences.
Author | : David D. Weis |
Publisher | : John Wiley & Sons |
Total Pages | : 376 |
Release | : 2016-01-12 |
Genre | : Science |
ISBN | : 1118703731 |
Hydrogen exchange mass spectrometry is widely recognized for its ability to probe the structure and dynamics of proteins. The application of this technique is becoming widespread due to its versatility for providing structural information about challenging biological macromolecules such as antibodies, flexible proteins and glycoproteins. Although the technique has been around for 25 years, this is the first definitive book devoted entirely to the topic. Hydrogen Exchange Mass Spectrometry of Proteins: Fundamentals, Methods and Applications brings into one comprehensive volume the theory, instrumentation and applications of Hydrogen Exchange Mass Spectrometry (HX-MS) - a technique relevant to bioanalytical chemistry, protein science and pharmaceuticals. The book provides a solid foundation in the basics of the technique and data interpretation to inform readers of current research in the method, and provides illustrative examples of its use in bio- and pharmaceutical chemistry and biophysics In-depth chapters on the fundamental theory of hydrogen exchange, and tutorial chapters on measurement and data analysis provide the essential background for those ready to adopt HX-MS. Expert users may advance their current understanding through chapters on methods including membrane protein analysis, alternative proteases, millisecond hydrogen exchange, top-down mass spectrometry, histidine exchange and method validation. All readers can explore the diversity of HX-MS applications in areas such as ligand binding, membrane proteins, drug discovery, therapeutic protein formulation, biocomparability, and intrinsically disordered proteins.
Author | : Roza Maria Kamp |
Publisher | : Springer Science & Business Media |
Total Pages | : 311 |
Release | : 2012-12-06 |
Genre | : Science |
ISBN | : 3642592198 |
"Protein Structure Analysis - Preparation and Characterization" is a compilation of practical approaches to the structural analysis of proteins and peptides. Here, about 20 authors describe and comment on techniques for sensitive protein purification and analysis. These methods are used worldwide in biochemical and biotechnical research currently being carried out in pharmaceu tical and biomedical laboratories or protein sequencing facilities. The chapters have been written by scientists with extensive ex perience in these fields, and the practical parts are well documen ted so that the reader should be able to easily reproduce the described techniques. The methods compiled in this book were demonstrated in student courses and in the EMBO Practical Course on "Microsequence Analysis of Proteins" held in Berlin September 10-15, 1995. The topics also derived from a FEBS Workshop, held in Halkidiki, Thessaloniki, Greece, in April, 1995. Most of the authors participated in these courses as lecturers and tutors and made these courses extremely lively and successful. Since polypeptides greatly vary depending on their specific structure and function, strategies for their structural analysis must for the most part be adapted to each individual protein. Therefore, advantages and limitations of the experimen tal approaches are discussed here critically, so that the reader becomes familiar with problems that might be encountered.
Author | : Andrew Baird |
Publisher | : |
Total Pages | : 542 |
Release | : 1991 |
Genre | : Medical |
ISBN | : |
Author | : W. Andy Tao |
Publisher | : John Wiley & Sons |
Total Pages | : 449 |
Release | : 2019-07-10 |
Genre | : Science |
ISBN | : 1118970217 |
PROVIDES STRATEGIES AND CONCEPTS FOR UNDERSTANDING CHEMICAL PROTEOMICS, AND ANALYZING PROTEIN FUNCTIONS, MODIFICATIONS, AND INTERACTIONS—EMPHASIZING MASS SPECTROMETRY THROUGHOUT Covering mass spectrometry for chemical proteomics, this book helps readers understand analytical strategies behind protein functions, their modifications and interactions, and applications in drug discovery. It provides a basic overview and presents concepts in chemical proteomics through three angles: Strategies, Technical Advances, and Applications. Chapters cover those many technical advances and applications in drug discovery, from target identification to validation and potential treatments. The first section of Mass Spectrometry-Based Chemical Proteomics starts by reviewing basic methods and recent advances in mass spectrometry for proteomics, including shotgun proteomics, quantitative proteomics, and data analyses. The next section covers a variety of techniques and strategies coupling chemical probes to MS-based proteomics to provide functional insights into the proteome. In the last section, it focuses on using chemical strategies to study protein post-translational modifications and high-order structures. Summarizes chemical proteomics, up-to-date concepts, analysis, and target validation Covers fundamentals and strategies, including the profiling of enzyme activities and protein-drug interactions Explains technical advances in the field and describes on shotgun proteomics, quantitative proteomics, and corresponding methods of software and database usage for proteomics Includes a wide variety of applications in drug discovery, from kinase inhibitors and intracellular drug targets to the chemoproteomics analysis of natural products Addresses an important tool in small molecule drug discovery, appealing to both academia and the pharmaceutical industry Mass Spectrometry-Based Chemical Proteomics is an excellent source of information for readers in both academia and industry in a variety of fields, including pharmaceutical sciences, drug discovery, molecular biology, bioinformatics, and analytical sciences.
Author | : Slavica Jonic |
Publisher | : Frontiers Media SA |
Total Pages | : 128 |
Release | : 2019-01-24 |
Genre | : |
ISBN | : 2889456994 |
Models of biomolecular structure and dynamics are often obtained by combining simulation or prediction approaches (e.g., comparative modeling, Molecular Dynamics (MD) simulations, Normal Mode Analysis (NMA), etc.) with experimental approaches (e.g., Nuclear Magnetic Resonance (NMR), X-ray crystallography, Small-Angle X-ray Scattering (SAXS), Electron Microscopy (EM), etc.). Such hybrid modeling extends the capabilities of experimental techniques, by enriching structural information and facilitating dynamics studies of biomolecules. This eBook contains articles on methodological developments, applications, and challenges of hybrid biomolecular modeling that have been collected in the framework of the Frontiers Research Topic entitled “Hybrid Biomolecular Modeling”.
Author | : Munishwar Nath Gupta |
Publisher | : Elsevier |
Total Pages | : 529 |
Release | : 2022-11-17 |
Genre | : Science |
ISBN | : 0323995349 |
Structure and Intrinsic Disorder in Enzymology offers a direct, yet comprehensive presentation of the fundamental concepts, characteristics and functions of intrinsically disordered enzymes, along with valuable notes and technical insights powering new research in this emerging field. Here, more than twenty international experts examine protein flexibility and cryo-enzymology, hierarchies of intrinsic disorder, methods for measurement of disorder in proteins, bioinformatics tools for predictions of structure, disorder and function, protein promiscuity, protein moonlighting, globular enzymes, intrinsic disorder and allosteric regulation, protein crowding, intrinsic disorder in post-translational, and much more. Chapters also review methods for study, as well as evolving technology to support new research across academic, industrial and pharmaceutical labs. - Unifies the roles of intrinsic disorder and structure in the functioning of enzymes and proteins - Examines a range of enzyme and protein characteristics, their relationship to intrinsic disorder, and methods for study - Features chapter contributions from international leaders in the field
Author | : Richard B. Cole |
Publisher | : Wiley-Interscience |
Total Pages | : 610 |
Release | : 1997-05-06 |
Genre | : Science |
ISBN | : |
Comprehensive, up-to-date coverage of a revolutionary technique Electrospray ionization mass spectrometry (ESI-MS) has completely changed the way physicists, chemists, and biologists view the study of large molecules. The technique derives detailed information about molecular weights and structures from extremely small sample quantities. ESI-MS can create highly charged forms of very high molecular weight compounds, it is naturally compatible with many types of separation techniques, and it allows noncovalent interactions between molecules in solution to be preserved in the gas phase. But many researchers may not use the technique to its full potential because they are unfamiliar with the different perspectives of its underlying processes, the varied approaches to implementation, and the wide-ranging utility of the technique. In this book, Richard B. Cole and an assemblage of leading researchers present a single-volume compilation of different approaches to the understanding and exploitation of ESI-MS. This comprehensive guide: * Examines the physical and chemical aspects of the electrospray process and describes the events involved in ion formation as well as the electro-chemical phenomena that are central to charged droplet formation during the process * Explores the coupling of electrospray ionization to various mass spectrometers, including quadrupole, magnetic, time-of-flight, quadrupole ion trap, and Fourier transform ion cyclotron resonance instruments * Describes recent progress in interfacing ESI with solution-based separation techniques, including liquid chromatography and capillary electrophoresis * Charts the rapid development of ESI applications and categorizes them by compound type: peptides and proteins, nucleic acids and their constituents, carbohydrates and lipids, small molecules related to pharmacology and drug metabolism, and organometallics and inorganic compounds Electrospray Ionization Mass Spectrometry is the indispensable handbook and reference for anyone who wishes to understand, implement, or apply this technique, including researchers in chemistry, metallochemistry, biochemistry, biology, pharmacology, and physics.
Author | : Gregory R. Bowman |
Publisher | : Springer Science & Business Media |
Total Pages | : 148 |
Release | : 2013-12-02 |
Genre | : Science |
ISBN | : 9400776063 |
The aim of this book volume is to explain the importance of Markov state models to molecular simulation, how they work, and how they can be applied to a range of problems. The Markov state model (MSM) approach aims to address two key challenges of molecular simulation: 1) How to reach long timescales using short simulations of detailed molecular models. 2) How to systematically gain insight from the resulting sea of data. MSMs do this by providing a compact representation of the vast conformational space available to biomolecules by decomposing it into states sets of rapidly interconverting conformations and the rates of transitioning between states. This kinetic definition allows one to easily vary the temporal and spatial resolution of an MSM from high-resolution models capable of quantitative agreement with (or prediction of) experiment to low-resolution models that facilitate understanding. Additionally, MSMs facilitate the calculation of quantities that are difficult to obtain from more direct MD analyses, such as the ensemble of transition pathways. This book introduces the mathematical foundations of Markov models, how they can be used to analyze simulations and drive efficient simulations, and some of the insights these models have yielded in a variety of applications of molecular simulation.