Physical Principles and Techniques of Protein Chemistry, Part 1 |
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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
08 Ribonuclease chromophores in , exposure of , 144 - 145 conformation
changes in , by fluores - cence , 226 - 227 , 229 2 ' - cytidylic acid binding by , 491
denaturation of difference spectra for , 136 - 139 rates of , 280 , 288 difference
spectra ...
08 Ribonuclease chromophores in , exposure of , 144 - 145 conformation
changes in , by fluores - 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 components concentration constant containing corrected corresponding curve dependence determined dielectric difference diffusion dipole direction distribution effect electric field electron electrophoresis elution emission energy equation equilibrium et al example excitation experimental experiments factor flow fluorescence fraction frequency function gel filtration given groups important increase indicate intensity interactions interpretation ionic strength ions light limited macromolecules measured method migration mixture mobility molecular molecules moving-boundary observed obtained occurs optical orientation particles patterns peaks perturbation phase plot polarization position possible present procedure produced protein ratio reaction reference relative relaxation respectively rotational separation serum albumin shown single solution solvent specific spectra spectrum structure studies technique theoretical theory tion unit usually values volume wavelength weight yield zone