Physical Principles and Techniques of Protein Chemistry Part B, Part 2Sydney Leach Physical Principles and Techniques of Protein Chemistry, Part B deals with the theories and application of selected physical methods in protein chemistry evaluation. This book is divided into seven chapters that cover the ultracentrifugal analysis, light scattering, infrared (IR) methods, nuclear magnetic resonance (NMR) spectroscopy, and differential thermal analysis of protein properties. This text first describes the fundamental ideas and methodology of sedimentation analysis of ideal noninteracting solutes and the problems of nonideality and solute-solute interaction. This book then deals with the problems involved in the interpretation of viscometric data for evaluation of intrinsic viscosity of proteins. The following chapters examine the principles, measurement and analysis of spectra, and experimental techniques of light scattering, IR, and NMR spectroscopic methods. Discussions on coordination phenomena, identification of binding sites, and ion binding in the crystalline state and in protein solutions are included. The concluding chapter presents some examples of protein analysis using differential thermal analysis technique. This book is of great value to chemists, biologists, and researchers who have great appreciation of protein chemistry. |
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Page 17
... observed for several self - inter- acting systems studied by sedimentation equilibrium ( see Section VII , C , 2,6 ) . In order to extend the range of concentrations that may be used in the ultracentrifuge , cells with optical path ...
... observed for several self - inter- acting systems studied by sedimentation equilibrium ( see Section VII , C , 2,6 ) . In order to extend the range of concentrations that may be used in the ultracentrifuge , cells with optical path ...
Page 35
... observed peaks may be used to specify the initial concentration of solute if cor- rected for the sectorial dilution that occurs during sedimentation . The simplest procedure is to measure the area under the schlieren peak for each ...
... observed peaks may be used to specify the initial concentration of solute if cor- rected for the sectorial dilution that occurs during sedimentation . The simplest procedure is to measure the area under the schlieren peak for each ...
Page 68
... observed both for insulin ( Adams and Fujita , 1963 ; Jeffrey and Coates , 1966b ) and lysozyme ( Adams and Filmer , 1966 ) . A satisfactory explana- tion has not yet been found , but the phenomenon may be a consequence of an effect of ...
... observed both for insulin ( Adams and Fujita , 1963 ; Jeffrey and Coates , 1966b ) and lysozyme ( Adams and Filmer , 1966 ) . A satisfactory explana- tion has not yet been found , but the phenomenon may be a consequence of an effect of ...
Page 77
... observed will not usually be that for zero concentration . When the optical detection method is sufficiently sensitive , it may be possible to use a 30 mm path length cell and hence reduce the concentration until the sedimenting zone ...
... observed will not usually be that for zero concentration . When the optical detection method is sufficiently sensitive , it may be possible to use a 30 mm path length cell and hence reduce the concentration until the sedimenting zone ...
Page 126
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Contents
1 | |
Chapter 11 Viscosity | 99 |
Chapter 12 Light Scattering | 147 |
Chapter 13 Infrared Methods | 213 |
Chapter 14 Nuclear Magnetic Resonance Spectroscopy | 275 |
Chapter 15 Binding of Protons and Other Ions | 365 |
Chapter 16 Differential Thermal Analysis | 437 |
Author Index | 463 |
Subject Index | 479 |
Common terms and phrases
absorption anions atoms band beam binding Biochemistry Biol bond bound Bradbury calculated cell chain changes Chem chemical shifts cm-ยน coil complex component concentration conformational constant copper(II crystalline denaturation density gradient dependence determined differential thermal analysis effect electron enzyme equation equilibrium field Fraser frequency fringe Gurd histidine hydrogen ion imidazole imidazole groups instrument interaction intrinsic viscosity Jardetzky ligand light scattering light-scattering line width lysozyme macromolecule magnetic measured meniscus metal ion method molecular weight molecule myoglobin Natl nuclei observed obtained optical density orientation parameters partial specific volume particle peak peptide Phys Polymer Polymer Sci Proc protein solution protons random coil reaction reference refractive index region relaxation residues resonance RNase rotation rotor sample schlieren Section sedimentation coefficient slit solvent spectra spectrum speed structure studies Tanford technique temperature thermogram Timasheff tion titration transition transmittance ultracentrifuge values velocity Vinograd viscometer zero