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 184
... give in detail some procedures and modifications that we have found effective and easily learned . This instrument gives absolute turbidities using a light beam 1.20 cm high and 1.20 cm wide in the optical cell , the latter being either ...
... give in detail some procedures and modifications that we have found effective and easily learned . This instrument gives absolute turbidities using a light beam 1.20 cm high and 1.20 cm wide in the optical cell , the latter being either ...
Page 195
... give information sufficient to characterize molecular weights , equilibrium constants , and virial coefficients in some protein systems ( Townend et al . , 1960 ; Tima- sheff and Townend , 1961a , b ) . One must be dealing , however ...
... give information sufficient to characterize molecular weights , equilibrium constants , and virial coefficients in some protein systems ( Townend et al . , 1960 ; Tima- sheff and Townend , 1961a , b ) . One must be dealing , however ...
Page 300
... give the swept- field spectrum is then computed from the accumulated spectrum . The method should be particularly suitable for protein PMR spectroscopy , and the rate at which spectra can be accumulated should be increased by a factor ...
... give the swept- field spectrum is then computed from the accumulated spectrum . The method should be particularly suitable for protein PMR spectroscopy , and the rate at which spectra can be accumulated should be increased by a factor ...
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