Physical Principles and Techniques of Protein ChemistryPhysical Principles and Techniques of Protein Chemistry Part C ... |
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Page 360
The steady - state birefringence is plotted against the square of the field strength
in Fig . 12 . Very large deviation from the Kerr law is observed ; saturation of the
birefringence is almost complete at the field strength of 4 . 2 X 103 V / cm .
The steady - state birefringence is plotted against the square of the field strength
in Fig . 12 . Very large deviation from the Kerr law is observed ; saturation of the
birefringence is almost complete at the field strength of 4 . 2 X 103 V / cm .
Page 392
Concentrations and boundary displacements for a hypothetical electrophoretic
experiment with a solution containing equal amounts of two proteins S and T (
Alberty , 1948a ) using sodium diethylbarbiturate buffer ( pH 8 . 6 , ionic strength
0 .
Concentrations and boundary displacements for a hypothetical electrophoretic
experiment with a solution containing equal amounts of two proteins S and T (
Alberty , 1948a ) using sodium diethylbarbiturate buffer ( pH 8 . 6 , ionic strength
0 .
Page 393
Extrapolation of apparent electrophoretic analysis at various protein
concentrations and salt concentrations to " ideal conditions ” ( Alberty , 1948a ) :
% P = protein concentration ( % by weight ) , r = ionic strength . concentration is
decreased ...
Extrapolation of apparent electrophoretic analysis at various protein
concentrations and salt concentrations to " ideal conditions ” ( Alberty , 1948a ) :
% P = protein concentration ( % by weight ) , r = ionic strength . concentration is
decreased ...
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Contents
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Examples of the Application of Electron Microscopy to the Study | 48 |
Copyright | |
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absorbance absorption acid appears applied atoms axis binding birefringence boundary buffer calculated cell charge Chem chromophores complex concentration constant containing contrast corrected corresponding curve decrease dependence determined dielectric difference diffusion dipole direction discussed distribution effect electric electric field electron electrophoresis emission energy equation equilibrium example excitation experimental experiments factor fluorescence fraction frequency function given groups Herskovits important increase indicates intensity interactions ionic ions length light limited macromolecules measured method mobility molecular molecules observed obtained occurs optical orientation particles patterns peaks perturbation phase phenolic polarization position possible preparation present produced protein quantum range ratio reaction reference relative relaxation respectively rotation sample separation serum albumin shift shown single solution solvent specimen spectra spectrum strength structure studies technique temperature theory tion transfer transition tryptophan unit usually volume wavelength yield zone