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Informationen zum Autor IGOR A. KALTASHOV, PHD, is a Professor in the Department of Chemistry at the University of Massachusetts Amherst. STEPHEN J. EYLES, PHD, is a Senior Lecturer in the Department of Biochemistry and Molecular Biology, and the Director of the Mass Spectrometry Center at the University of Massachusetts Amherst. Klappentext The definitive guide to mass spectrometry techniques in biology and biophysicsThe use of mass spectrometry (MS) to study the architecture and dynamics of proteins is increasingly common within the biophysical community, and Mass Spectrometry in Structural Biology and Biophysics: Architecture, Dynamics, and Interaction of Biomolecules, Second Edition provides readers with detailed, systematic coverage of the current state of the art.Offering an unrivalled overview of modern MS-based armamentarium that can be used to solve the most challenging problems in biophysics, structural biology, and biopharmaceuticals, the book is a practical guide to understanding the role of MS techniques in biophysical research. Designed to meet the needs of both academic and industrial researchers, it makes mass spectrometry accessible to professionals in a range of fields, including biopharmaceuticals.This new edition has been significantly expanded and updated to include the most recent experimental methodologies and techniques, MS applications in biophysics and structural biology, methods for studying higher order structure and dynamics of proteins, an examination of other biopolymers and synthetic polymers, such as nucleic acids and oligosaccharides, and much more.Featuring high-quality illustrations that illuminate the concepts described in the text, as well as extensive references that enable the reader to pursue further study, Mass Spectrometry in Structural Biology and Biophysics is an indispensable resource for researchers and graduate students working in biophysics, structural biology, protein chemistry, and related fields. Zusammenfassung With its detailed and systematic coverage of the current state of biophysical mass spectrometry (MS), here is one of the first systematic presentations of the full experimental array of MS-based techniques used in biophysics, covering both fundamental and practical issues. Inhaltsverzeichnis Preface to the Second Edition xi Preface to the First Edition xiii 1 General Overview of Basic Concepts in Molecular Biophysics 1 1.1 Covalent Structure of Biopolymers, 1 1.2 Noncovalent Interactions and Higher Order Structure, 3 1.2.1 Electrostatic Interaction, 3 1.2.2 Hydrogen Bonding, 6 1.2.3 Steric Clashes and Allowed Conformations of the Peptide Backbone: Secondary Structure, 6 1.2.4 Solvent--Solute Interactions, Hydrophobic Effect, Side-Chain Packing, and Tertiary Structure, 7 1.2.5 Intermolecular Interactions and Association: Quaternary Structure, 9 1.3 The Protein Folding Problem, 9 1.3.1 What Is Protein Folding?, 9 1.3.2 Why Is Protein Folding So Important?, 10 1.3.3 What Is the Natively Folded Protein and How Do We Define a Protein Conformation?, 11 1.3.4 What Are Non-Native Protein Conformations?: Random Coils, Molten Globules, and Folding Intermediates, 12 1.3.5 Protein Folding Pathways, 13 1.4 Protein Energy Landscapes and the Folding Problem, 14 1.4.1 Protein Conformational Ensembles and Energy Landscapes: Enthalpic and Entropic Considerations, 14 1.4.2 Equilibrium and Kinetic Intermediates on the Energy Landscape, 16 1.5 Protein Dynamics and Function, 17 1.5.1 Limitations of the Structure--Function Paradigm, 17 1.5.2 Protein Dynamics under Native Conditions, 17 1.5.3 Is Well-Defined Structure Required for Functional Competence?, 18 1.5.4 Biomolecular Dynamics and Binding from The Energy Landscape Perspective, 19 1.5.5 Energ...
