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 70
... Vinograd et al . ( 1963 ) the solution is placed onto solvent of uniform concentration and a density gradient is generated by the diffusion of small molecules at a relatively high concentration in the solvent layer into the solution ...
... Vinograd et al . ( 1963 ) the solution is placed onto solvent of uniform concentration and a density gradient is generated by the diffusion of small molecules at a relatively high concentration in the solvent layer into the solution ...
Page 72
... Vinograd and Bruner ( 1966b ) , shows how the concentra- tion of the zone maximum changes with time for solutes with various diffusion coefficients . It is apparent that for most proteins ( D≈ 10-6 ) the rate of diffusion is relatively ...
... Vinograd and Bruner ( 1966b ) , shows how the concentra- tion of the zone maximum changes with time for solutes with various diffusion coefficients . It is apparent that for most proteins ( D≈ 10-6 ) the rate of diffusion is relatively ...
Page 73
... Vinograd and Bruner , 1966b ) . ( Reproduced by courtesy of the copyright owner , John Wiley and Sons . ) solute are described in detail by Vinograd and Bruner ( 1966b ) . The fol- lowing general principles emerge : the maximum negative ...
... Vinograd and Bruner , 1966b ) . ( Reproduced by courtesy of the copyright owner , John Wiley and Sons . ) solute are described in detail by Vinograd and Bruner ( 1966b ) . The fol- lowing general principles emerge : the maximum negative ...
Page 74
... Vinograd and Bruner , 1966b ) . ( Reproduced by courtesy of the copy- right owner , John Wiley and Sons . ) overtake the steep part of the diffusion gradient in its movement down the cell . This consideration places an upper limit on ...
... Vinograd and Bruner , 1966b ) . ( Reproduced by courtesy of the copy- right owner , John Wiley and Sons . ) overtake the steep part of the diffusion gradient in its movement down the cell . This consideration places an upper limit on ...
Page 75
... Vinograd and Bruner ( 1966c ) ( see also Section VIII , C , 6 ) . For the lowest possible concentration with maximum optical sensitivity , the 30 - mm optical path length cell is to be preferred . Twenty - five microliters of solution ...
... Vinograd and Bruner ( 1966c ) ( see also Section VIII , C , 6 ) . For the lowest possible concentration with maximum optical sensitivity , the 30 - mm optical path length cell is to be preferred . Twenty - five microliters of solution ...
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-¹ 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