Physical Principles and Techniques of Protein ChemistryPhysical Principles and Techniques of Protein Chemistry Part C ... |
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Page 154
The optimum absorbance ( that absorbance giving the smallest relative error of
measurement ) with a shot - noise limited system is about 1 . 0 ( Fig . 21 ) .
However , samples with absorbances of 2 or 3 are measured nearly as
accurately . 0 .
The optimum absorbance ( that absorbance giving the smallest relative error of
measurement ) with a shot - noise limited system is about 1 . 0 ( Fig . 21 ) .
However , samples with absorbances of 2 or 3 are measured nearly as
accurately . 0 .
Page 230
Fluorescence may be used in approximately the same way as absorption to
evaluate the relative exposure of fluorochromes in proteins to the ambient solvent
. In effect , any molecule that changes the quantum yield of fluorescence without ...
Fluorescence may be used in approximately the same way as absorption to
evaluate the relative exposure of fluorochromes in proteins to the ambient solvent
. In effect , any molecule that changes the quantum yield of fluorescence without ...
Page 480
Studies of Rapid Chemical Equilibria In studies of interacting protein systems by
gel filtration the effects of the chemical reaction upon the elution profiles vary
according to the equilibrium position and the rate of re - equilibration relative to
that ...
Studies of Rapid Chemical Equilibria In studies of interacting protein systems by
gel filtration the effects of the chemical reaction upon the elution profiles vary
according to the equilibrium position and the rate of re - equilibration relative to
that ...
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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