LEADER 05697nam 2200769Ia 450 001 9911020041503321 005 20200520144314.0 010 $a9786613620118 010 $a9781280590283 010 $a1280590289 010 $a9781118232118 010 $a1118232119 010 $a9781118232125 010 $a1118232127 035 $a(CKB)2670000000160785 035 $a(EBL)832583 035 $a(SSID)ssj0000622294 035 $a(PQKBManifestationID)11385801 035 $a(PQKBTitleCode)TC0000622294 035 $a(PQKBWorkID)10638258 035 $a(PQKB)11644443 035 $a(MiAaPQ)EBC832583 035 $a(MiAaPQ)EBC4033067 035 $a(OCoLC)779616869 035 $a(Perlego)1013463 035 $a(EXLCZ)992670000000160785 100 $a20111026d2012 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 10$aMass spectrometry in structural biology and biophysics $earchitecture, dynamics, and interaction of biomolecules /$fIgor A. Kaltashov, Stephen J. Eyles 205 $a2nd ed. 210 $aHoboken, N.J. $cWiley$dc2012 215 $a1 online resource (312 p.) 225 0 $aWiley series on mass spectrometry 300 $aDescription based upon print version of record. 311 08$a9781118232088 311 08$a1118232089 311 08$a9780470937792 311 08$a0470937793 320 $aIncludes bibliographical references and index. 327 $aMASS SPECTROMETRY IN STRUCTURAL BIOLOGY AND BIOPHYSICS: Architecture, Dynamics, and Interaction of Biomolecules; CONTENTS; Preface to the Second Edition; Preface to the First Edition; 1 General Overview of Basic Concepts in Molecular Biophysics; 1.1 Covalent Structure of Biopolymers; 1.2 Noncovalent Interactions and Higher Order Structure; 1.2.1 Electrostatic Interaction; 1.2.2 Hydrogen Bonding; 1.2.3 Steric Clashes and Allowed Conformations of the Peptide Backbone: Secondary Structure; 1.2.4 Solvent--Solute Interactions, Hydrophobic Effect, Side-Chain Packing, and Tertiary Structure 327 $a1.2.5 Intermolecular Interactions and Association: Quaternary Structure1.3 The Protein Folding Problem; 1.3.1 What Is Protein Folding?; 1.3.2 Why Is Protein Folding So Important?; 1.3.3 What Is the Natively Folded Protein and How Do We Define a Protein Conformation?; 1.3.4 What Are Non-Native Protein Conformations?: Random Coils, Molten Globules, and Folding Intermediates; 1.3.5 Protein Folding Pathways; 1.4 Protein Energy Landscapes and the Folding Problem; 1.4.1 Protein Conformational Ensembles and Energy Landscapes: Enthalpic and Entropic Considerations 327 $a1.4.2 Equilibrium and Kinetic Intermediates on the Energy Landscape1.5 Protein Dynamics and Function; 1.5.1 Limitations of the Structure--Function Paradigm; 1.5.2 Protein Dynamics under Native Conditions; 1.5.3 Is Well-Defined Structure Required for Functional Competence?; 1.5.4 Biomolecular Dynamics and Binding from The Energy Landscape Perspective; 1.5.5 Energy Landscapes Within a Broader Context of Nonlinear Dynamics: Information Flow and Fitness Landscapes; 1.6 Protein Higher Order Structure and Dynamics from A Biotechnology Perspective; References 327 $a2 Overview of Traditional Experimental Arsenal to Study Biomolecular Structure and Dynamics2.1 X-Ray Crystallography; 2.1.1 Fundamentals; 2.1.2 Crystal Structures at Atomic and Ultrahigh Resolution; 2.1.3 Crystal Structures of Membrane Proteins; 2.1.4 Protein Dynamics and X-Ray Diffraction; 2.2 Solution Scattering Techniques; 2.2.1 Static and Dynamic Light Scattering; 2.2.2 Small-Angle X-Ray Scattering; 2.2.3 Cryo-Electron Microscopy; 2.2.4 Neutron Scattering; 2.3 NMR Spectroscopy; 2.3.1 Heteronuclear NMR; 2.3.2 Hydrogen Exchange by NMR; 2.4 Other Spectroscopic Techniques 327 $a2.4.1 Cumulative Measurements of Higher Order Structure: Circular Dichroism2.4.2 Vibrational Spectroscopy; 2.4.3 Fluorescence: Monitoring Specific Dynamic Events; 2.5 Other Biophysical Methods to Study Macromolecular Interactions and Dynamics; 2.5.1 Calorimetric Methods; 2.5.2 Analytical Ultracentrifugation; 2.5.3 Surface Plasmon Resonance; 2.5.4 Size Exclusion Chromatography (Gel Filtration); 2.5.5 Electrophoresis; 2.5.6 Affinity Chromatography; References; 3 Overview of Biological Mass Spectrometry; 3.1 Basic Principles of Mass Spectrometry; 3.1.1 Stable Isotopes and Isotopic Distributions 327 $a3.1.2 Macromolecular Mass: Terms and Definitions 330 $a The definitive guide to mass spectrometry techniques in biology and biophysics The use of mass spectrometry (MS) to study the architecture and dynamics of proteins is increasingly common within the biophysical community, and Mass Spectrometry in Structural Biology and Biophysics: Architecture, Dynamics, and Interaction of Biomolecules, Second Edition provides readers with detailed, systematic coverage of the current state of the art. Offering an unrivalled overview of modern MS-based armamentarium that can be used to solve the most challenging problems in biophysics, structural biol 410 0$aWiley-Interscience series on mass spectrometry. 606 $aMass spectrometry 606 $aBiophysics 606 $aBiomolecules$xSpectra 615 0$aMass spectrometry. 615 0$aBiophysics. 615 0$aBiomolecules$xSpectra. 676 $a610.28/4 700 $aKaltashov$b Igor A$0873998 701 $aEyles$b Stephen J$01840611 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9911020041503321 996 $aMass spectrometry in structural biology and biophysics$94420199 997 $aUNINA