Physical Principles and Techniques of Protein Chemistry, Part 1 |
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Page 133
O2H|O 3O 50 7O pH Fig. 12. Solvent perturbation of the phenolic chromophores
in native ribonuclease, ribonuclease in 8 M urea, and thioglycolic acid reduced
ribonuclease in 8 M urea. Perturbants: 10% and 20% glycerol. The ordinate is the
...
O2H|O 3O 50 7O pH Fig. 12. Solvent perturbation of the phenolic chromophores
in native ribonuclease, ribonuclease in 8 M urea, and thioglycolic acid reduced
ribonuclease in 8 M urea. Perturbants: 10% and 20% glycerol. The ordinate is the
...
Page 134
This appears to be in agreement with spectrophotometric titrations, which show
that three phenolic groups in ribonuclease are normal, and three abnormal (
Shugar, 1952; Tanford et al., 1955). Perturbation of ribonuclease in 8 M urea
indicates ...
This appears to be in agreement with spectrophotometric titrations, which show
that three phenolic groups in ribonuclease are normal, and three abnormal (
Shugar, 1952; Tanford et al., 1955). Perturbation of ribonuclease in 8 M urea
indicates ...
Page 137
An example of the exposure of chromophores upon denaturation of ribonuclease
is shown in Fig. 14. With low concentrations of guanidinium chloride (GCl), at
which unfolding of the protein does not occur, a small red shift in the spectrum of
...
An example of the exposure of chromophores upon denaturation of ribonuclease
is shown in Fig. 14. With low concentrations of guanidinium chloride (GCl), at
which unfolding of the protein does not occur, a small red shift in the spectrum of
...
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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