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
... values to standard conditions ( Section IV , B , 4 ) . Where sedimentation coefficient values are being extrap- olated to zero concentration , the viscosity and density of the solvent at the temperatures of the various experiments will ...
... values to standard conditions ( Section IV , B , 4 ) . Where sedimentation coefficient values are being extrap- olated to zero concentration , the viscosity and density of the solvent at the temperatures of the various experiments will ...
Page 279
... values . The number of different values observed was ( 21+ 1 ) where I is the spin number , which may have the value 0 , 1⁄2 , 1 , 2 , . . . depending on the particular isotopic nucleus . The finding of discrete values for the magnetic ...
... values . The number of different values observed was ( 21+ 1 ) where I is the spin number , which may have the value 0 , 1⁄2 , 1 , 2 , . . . depending on the particular isotopic nucleus . The finding of discrete values for the magnetic ...
Page 383
... values of n that yielded closely comparable values of w . Apply- ing Eq . ( 2 ) , pKa was read off at the point corresponding to Z equal to 0 . Because of restrictions on the range of pH in which the protein is stable , experimental values ...
... values of n that yielded closely comparable values of w . Apply- ing Eq . ( 2 ) , pKa was read off at the point corresponding to Z equal to 0 . Because of restrictions on the range of pH in which the protein is stable , experimental values ...
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