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 167
... molar scale , bovine serum albumin has an apparent light - scattering molec- ular weight , M2 ( 1 + D ) 2 of 38,000 , while in dilute salt the molecular weight M2 of the same sample is 76,000 ( Noelken and Timasheff , 1967 ) ( see Fig ...
... molar scale , bovine serum albumin has an apparent light - scattering molec- ular weight , M2 ( 1 + D ) 2 of 38,000 , while in dilute salt the molecular weight M2 of the same sample is 76,000 ( Noelken and Timasheff , 1967 ) ( see Fig ...
Page 347
... molar ratio of inhibitor to enzyme is approximately 3. Peaks of the inhibitor are identified by H6 and H1 ' . ( d ) Selectively deuterated analog of nuclease ( 6 % ) plus the inhibitor 3 ' , 5 ' - thymidine diphosphate ( molar ratio of ...
... molar ratio of inhibitor to enzyme is approximately 3. Peaks of the inhibitor are identified by H6 and H1 ' . ( d ) Selectively deuterated analog of nuclease ( 6 % ) plus the inhibitor 3 ' , 5 ' - thymidine diphosphate ( molar ratio of ...
Page 485
... Molar absorptivity , definition of , 227 Molar volume of reaction , 60 Molecular weights apparent , in sedimentation , 52–53 errors in , due to preferential binding , 166 light scattering and , 153 , 159 , 162-167 , 171 , 195 NMR of ...
... Molar absorptivity , definition of , 227 Molar volume of reaction , 60 Molecular weights apparent , in sedimentation , 52–53 errors in , due to preferential binding , 166 light scattering and , 153 , 159 , 162-167 , 171 , 195 NMR of ...
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