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 37
... ionic strength 0.1 , or better 0.2 , should be used as solvent for a 1 % protein solution . If high ionic strength causes precipitation of any solute material , lower ionic strengths may be used , but the protein concentration must be ...
... ionic strength 0.1 , or better 0.2 , should be used as solvent for a 1 % protein solution . If high ionic strength causes precipitation of any solute material , lower ionic strengths may be used , but the protein concentration must be ...
Page 126
... ionic atmosphere surrounding the polyions unchanged during the dilution process . If the reasonable assumption is made that the fixed charges on the polyelectrolyte act as univalent ions ... strength ; this process is called isoionic dilution ...
... ionic atmosphere surrounding the polyions unchanged during the dilution process . If the reasonable assumption is made that the fixed charges on the polyelectrolyte act as univalent ions ... strength ; this process is called isoionic dilution ...
Page 366
... ionic milieu . Control of pH and of ionic strength , which determine the average charge distributions on the proteins and the effective ranges of the electric fields around those charges , makes it possible to control electrophoretic ...
... ionic milieu . Control of pH and of ionic strength , which determine the average charge distributions on the proteins and the effective ranges of the electric fields around those charges , makes it possible to control electrophoretic ...
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