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 297
... changes in the measured re- laxation times can be interpreted as selective changes in correlation times , it is necessary to show that it is only changes in the correlation times which are affecting relaxation on complex formation . We ...
... changes in the measured re- laxation times can be interpreted as selective changes in correlation times , it is necessary to show that it is only changes in the correlation times which are affecting relaxation on complex formation . We ...
Page 415
... Changes Related to lon Binding Although an ion binding site may be exactly preformed in a protein , one may expect that often it will not be . In such cases a conformational change of some magnitude will be required to accommodate the ...
... Changes Related to lon Binding Although an ion binding site may be exactly preformed in a protein , one may expect that often it will not be . In such cases a conformational change of some magnitude will be required to accommodate the ...
Page 419
... change in peptide conformation . B. TIME - DEPENDENT CHANGES IN COMPLEXES 1. Course of Alterations in Myoglobin Complexes In contrast to the minimal alteration in protein structure occasioned by the binding of one equivalent of copper ...
... change in peptide conformation . B. TIME - DEPENDENT CHANGES IN COMPLEXES 1. Course of Alterations in Myoglobin Complexes In contrast to the minimal alteration in protein structure occasioned by the binding of one equivalent of copper ...
Contents
Ultracentrifugal Analysis | 10 |
Light Scattering | 12 |
Osmotic Pressure | 13 |
Copyright | |
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absorption acid angle axial ratio axis band beam binding Biol Bradbury Brice calculated capillary centrifugal chain Chem chemical shifts column complex component concentration dependence constant copper(II denaturation density gradient determined diffusion dilution Doty effect ellipsoid equation experiments extrapolation filters Fraser frequency fringe groups Gurd Holtzer hydrogen increment instrument interaction intrinsic viscosity Kirkwood length light scattering light-scattering linear macromolecule maximum measured meniscus method molecular weight molecule Natl observed obtained optical density optical system parameters partial specific volume particle peak photographic Phys plate plateau plot Polymer Sci Proc procedure protein solution protons radius random coil Rayleigh reference refractive index refractive index increment residues resonance rotation rotor sample Schachman schlieren Section sedimentation coefficient sedimentation equilibrium shearing stress shown in Fig slit solvent spectra spectrum speed structure synthetic boundary Tanford technique temperature Timasheff tion transmittance tube ultracentrifuge values Vinograd viscometer zero Zimm zone