Physical Principles and Techniques of Protein ChemistryPhysical Principles and Techniques of Protein Chemistry Part C ... |
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Page 122
V . Perturbation Difference Spectra Spectrophotometric observation of
perturbations of the chromophores of proteins has become a valuable method for
the determination of certain aspects of the conformation of native and denatured
proteins ...
V . Perturbation Difference Spectra Spectrophotometric observation of
perturbations of the chromophores of proteins has become a valuable method for
the determination of certain aspects of the conformation of native and denatured
proteins ...
Page 129
In the absence of conformational changes of the protein , only those groups
extending into the solvent are perturbed by this ... If the alteration in solvent
composition affects the conformation of the protein , then in addition to the
perturbation of ...
In the absence of conformational changes of the protein , only those groups
extending into the solvent are perturbed by this ... If the alteration in solvent
composition affects the conformation of the protein , then in addition to the
perturbation of ...
Page 226
Conformational Transitions The lifetime of the excited state is about 104 - 106
times greater than the time required for excitation . Reactions which are fast
enough to occur during the lifetime of the excited state but are too slow to
influence the ...
Conformational Transitions The lifetime of the excited state is about 104 - 106
times greater than the time required for excitation . Reactions which are fast
enough to occur during the lifetime of the excited state but are too slow to
influence the ...
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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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Common terms and phrases
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