Physical Principles and Techniques of Protein Chemistry, Part 1 |
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Page 125
A. PERTURBATION BY CHARGED GROUPs Chromophores in a protein can be
perturbed by adjacent positive or negative charges. Their spectra may thereby be
altered. Experimentally, as the negative charge is increased, it is found that ...
A. PERTURBATION BY CHARGED GROUPs Chromophores in a protein can be
perturbed by adjacent positive or negative charges. Their spectra may thereby be
altered. Experimentally, as the negative charge is increased, it is found that ...
Page 128
TABLE VIII CHARGE PERTURBATION of SPECTRA of Model CoMPounds
EFFECT of CoMPLETE DE-PROTONATION of THE IonizaBLE GROUPS"
Chromo- Ionizable max" Aea-amino Compound phore group (mu) Aemax (Ae/e)*
...
TABLE VIII CHARGE PERTURBATION of SPECTRA of Model CoMPounds
EFFECT of CoMPLETE DE-PROTONATION of THE IonizaBLE GROUPS"
Chromo- Ionizable max" Aea-amino Compound phore group (mu) Aemax (Ae/e)*
...
Page 376
The zeta potential is determined by the charge inside this surface. This charge is
not necessarily identical with the net charge of the particle, since some of the ions
of the ionic atmosphere may be present within the surface of shear, thereby ...
The zeta potential is determined by the charge inside this surface. This charge is
not necessarily identical with the net charge of the particle, since some of the ions
of the ionic atmosphere may be present within the surface of shear, thereby ...
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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