Physical Principles and Techniques of Protein Chemistry, Part 1 |
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Page 130
aqueous solvents on protein conformation have been reviewed by Singer (1962).
The spectra of chromophores exposed to water at the surface of a protein
molecule are “red-shifted” relative to the vapor spectrum, because of the
polarization ...
aqueous solvents on protein conformation have been reviewed by Singer (1962).
The spectra of chromophores exposed to water at the surface of a protein
molecule are “red-shifted” relative to the vapor spectrum, because of the
polarization ...
Page 146
If there is no chromophore near an active site, or near a region which undergoes
a conformational change, or on a surface at which association takes place, then
an artificial chromophore may be inserted by chemical modification of the protein
...
If there is no chromophore near an active site, or near a region which undergoes
a conformational change, or on a surface at which association takes place, then
an artificial chromophore may be inserted by chemical modification of the protein
...
Page 231
D. CoNJUGATED PROTEIN's 1. Eacperimental Proteins comprise a class of
molecules very suitable for study by the polarization of fluorescence method (
Section I,D) originally developed by Perrin. Many native proteins appear to be
rigid ...
D. CoNJUGATED PROTEIN's 1. Eacperimental Proteins comprise a class of
molecules very suitable for study by the polarization of fluorescence method (
Section I,D) originally developed by Perrin. Many native proteins appear to be
rigid ...
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Contents
Electron Microscopy | 2 |
Dielectric Properties of Proteins | 7 |
Operational Requirements for HighResolution Electron | 15 |
Copyright | |
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absorbance absorption acid albumin appears applied atoms axis binding birefringence boundary buffer calculated cell charge Chem chromophores concentration constant containing contrast corrected corresponding curve dependence determined dielectric difference diffusion dipole direction effect electric electric field electron electrophoresis emission energy equation equilibrium example excitation experimental experiments factor field flow fluorescence fraction frequency function given groups important increase indicates intensity interactions ionic ions length light limited macromolecules measured method microscope mobility molecular molecules observed obtained occurs optical particles patterns peaks perturbation phase polarization position possible preparation present produced protein range ratio reaction reference relative relaxation resolution respectively rotation sample separation serum shift shown single solution solvent specimen spectra spectrum strength structure studies technique temperature theory tion tryptophan unit usually values volume wavelength weight yield zone