Physical Principles and Techniques of Protein Chemistry, Part 2Sydney J. Leach, Sidney J. 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 ... |
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Page vii
... follow . This volume follows the pattern set by Part A of this treatise . Physical techniques which are well established in protein chemistry are described in a detailed but critical way . Other current techniques have demanded a more ...
... follow . This volume follows the pattern set by Part A of this treatise . Physical techniques which are well established in protein chemistry are described in a detailed but critical way . Other current techniques have demanded a more ...
Page 314
... follows the upfield shift of the CaH peak closely . 2 Bradbury et al . ( 1968a ) have examined the spectra of PBLG samples with a range of DP values to follow the effect of molecular weight on the PMR spectra in the helix - coil ...
... follows the upfield shift of the CaH peak closely . 2 Bradbury et al . ( 1968a ) have examined the spectra of PBLG samples with a range of DP values to follow the effect of molecular weight on the PMR spectra in the helix - coil ...
Page 367
... follows also that in most respects the binding of neutral polar molecules to proteins is fundamentally similar to that of ions . The subject of ion binding by proteins has become so broad in the number and variety of examples that much ...
... follows also that in most respects the binding of neutral polar molecules to proteins is fundamentally similar to that of ions . The subject of ion binding by proteins has become so broad in the number and variety of examples that much ...
Contents
Ultracentrifugal Analysis J H Coates | 1 |
Glossary of Symbols | 2 |
Introduction | 3 |
Copyright | |
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absorption acid amino anions atoms axial ratio band beam binding Biol bond Bradbury calculated capillary cell centrifugal chain changes Chem chemical shifts complex component concentration constant copper(II denaturation density gradient dependence determined dilution Doty effect electron ellipsoid enzyme equation extrapolation field Fraser frequency fringe Gurd histidine hydrogen ion imidazole imidazole groups instrument interaction intrinsic viscosity Jardetzky length light scattering light-scattering line width lysozyme macromolecule magnetic measured meniscus metal ion method molecular weight molecule myoglobin nuclei observed obtained optical density optical system partial specific volume particle PBLG peak peptide Phys plot Polymer Sci Proc protein solution protons random coil Rayleigh reference refractive index relaxation residues resonance RNase rotation rotor sample schlieren Section sedimentation coefficient sedimentation equilibrium shearing stress slit solvent spectra spectrum speed structure studies Tanford technique temperature Timasheff tion transition ultracentrifuge values velocity Vinograd viscometer zero zone