Physical Principles and Techniques of Protein Chemistry, Part 1 |
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Page 337
After leaving the medium, these two components recombine to form elliptically
polarized light. The magnitude of the electric birefringence is represented by An =
m1 — nil. Depending on the relative magnitude of n, and n_1, the birefringence ...
After leaving the medium, these two components recombine to form elliptically
polarized light. The magnitude of the electric birefringence is represented by An =
m1 — nil. Depending on the relative magnitude of n, and n_1, the birefringence ...
Page 339
Holcomb and Tinoco (1963) extended the birefringence saturation theory to the
most general molecular model, and applied it to an interpretation of the data on
fibrinogen. ll. Outline of Theory A. ELECTRIC BIREFRINGENCE We shall briefly ...
Holcomb and Tinoco (1963) extended the birefringence saturation theory to the
most general molecular model, and applied it to an interpretation of the data on
fibrinogen. ll. Outline of Theory A. ELECTRIC BIREFRINGENCE We shall briefly ...
Page 364
electric birefringence of PBLG in ethylene dichloride using the rectangular pulse
technique. The Kerr constant and the rotational diffusion constant were measured
as functions of the concentration for two samples of different molecular weight.
electric birefringence of PBLG in ethylene dichloride using the rectangular pulse
technique. The Kerr constant and the rotational diffusion constant were measured
as functions of the concentration for two samples of different molecular weight.
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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