Physical Principles and Techniques of Protein ChemistryPhysical Principles and Techniques of Protein Chemistry Part C ... |
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Page 144
Binding of DDS to serum albumin produces a negative difference spectrum in the
280 – 310 mu region ( Fig . 17 ) , resulting mainly or entirely from a blue shift in
the spectrum of the 2 indole and 21 phenolic chromophores , some of which are ...
Binding of DDS to serum albumin produces a negative difference spectrum in the
280 – 310 mu region ( Fig . 17 ) , resulting mainly or entirely from a blue shift in
the spectrum of the 2 indole and 21 phenolic chromophores , some of which are ...
Page 237
shift in the emission peak on binding of ANS , a similar trend was observed when
ANS was dissolved in a series of ... Though few proteins will bind this class of
dyes in their native state , denaturation will often lead to binding and marked ...
shift in the emission peak on binding of ANS , a similar trend was observed when
ANS was dissolved in a series of ... Though few proteins will bind this class of
dyes in their native state , denaturation will often lead to binding and marked ...
Page 526
20 Ribonuclease chromophores in , exposure of , 144 - 145 conformation
changes in , by Auores - cence , 226 - 227 , 229 2 - cytidylic acid binding by , 491
denaturation of difference spectra for , 136 - 139 rates of , 280 , 288 difference
spectra ...
20 Ribonuclease chromophores in , exposure of , 144 - 145 conformation
changes in , by Auores - cence , 226 - 227 , 229 2 - cytidylic acid binding by , 491
denaturation of difference spectra for , 136 - 139 rates of , 280 , 288 difference
spectra ...
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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