Physical Principles and Techniques of Protein Chemistry, Part 1 |
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Page 3
Unlike the glass lenses of the light microscope, electron lenses may be
continuously varied in strength (focal length) over a rather wide range. As in the
light microscope, a series of lenses—the condenser(s), objective, and projector (
the latter, ...
Unlike the glass lenses of the light microscope, electron lenses may be
continuously varied in strength (focal length) over a rather wide range. As in the
light microscope, a series of lenses—the condenser(s), objective, and projector (
the latter, ...
Page 348
calculate the parameter r from the initial slope of the buildup curve for sufficiently
low field strength by the relation dAn _ 60Ano - (#). T r + 1 (34) Another method
for determining the parameter r is the area method (Yoshioka and Watanabe, ...
calculate the parameter r from the initial slope of the buildup curve for sufficiently
low field strength by the relation dAn _ 60Ano - (#). T r + 1 (34) Another method
for determining the parameter r is the area method (Yoshioka and Watanabe, ...
Page 392
Concentrations and boundary displacements for a hypothetical electrophoretic
experiment with a solution containing equal amounts of two proteins S and T (
Alberty, 1948a) using sodium diethylbarbiturate buffer (pH 8.6, ionic strength 0.05
) ...
Concentrations and boundary displacements for a hypothetical electrophoretic
experiment with a solution containing equal amounts of two proteins S and T (
Alberty, 1948a) using sodium diethylbarbiturate buffer (pH 8.6, ionic strength 0.05
) ...
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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