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 36
... experiments will suffice instead of the corresponding values for the protein solution , since the solution values tend to ... experimental determination of density increments are described in Volume C of this series . The use of the ...
... experiments will suffice instead of the corresponding values for the protein solution , since the solution values tend to ... experimental determination of density increments are described in Volume C of this series . The use of the ...
Page 105
... experimental differences found by Ibrahim ( 1965 ) , it is perhaps worthwhile to check the extrapolation by use of Eq . ( 3 ) . According to Ibrahim and Elias ( 1964 ) , Eq . ( 4 ) should not be used because it gives incorrect values of ...
... experimental differences found by Ibrahim ( 1965 ) , it is perhaps worthwhile to check the extrapolation by use of Eq . ( 3 ) . According to Ibrahim and Elias ( 1964 ) , Eq . ( 4 ) should not be used because it gives incorrect values of ...
Page 174
... experiments give M2 , M4 , B22 and ẞ . Substitution of these values into Eq . ( 18 ) together with the experimental data of the interacting mixture gives ẞ42 , i.e. , the strength of the attrac- tion between the two proteins , and ( dg1 ...
... experiments give M2 , M4 , B22 and ẞ . Substitution of these values into Eq . ( 18 ) together with the experimental data of the interacting mixture gives ẞ42 , i.e. , the strength of the attrac- tion between the two proteins , and ( dg1 ...
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