Physical Principles and Techniques of Protein ChemistryPhysical Principles and Techniques of Protein Chemistry Part C ... |
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Page 303
Separating the real and imaginary parts and rearranging , we obtain ( 42 ) WT f "
= ( co – end ) 1 * " w273 ( 43 ) where eo and to are the dielectric constants at very
low and very high frequencies , respectively . The changes in é and as a ...
Separating the real and imaginary parts and rearranging , we obtain ( 42 ) WT f "
= ( co – end ) 1 * " w273 ( 43 ) where eo and to are the dielectric constants at very
low and very high frequencies , respectively . The changes in é and as a ...
Page 309
Another cause of error is due to an inductance ( Schwan , 1963 ) and this
becomes serious at higher frequencies . ... we may calculate the dielectric
constant e and the specific conductivity k of the solution at each frequency C =
eer ( A / 1 ) G ...
Another cause of error is due to an inductance ( Schwan , 1963 ) and this
becomes serious at higher frequencies . ... we may calculate the dielectric
constant e and the specific conductivity k of the solution at each frequency C =
eer ( A / 1 ) G ...
Page 324
D . High FREQUENCY DIELECTRIC CONSTANTS OF PROTEIN SOLUTIONS
The dielectric constants of protein solutions are slightly lower than that of water at
very high frequencies . This is because protein molecules behave like nonpolar ...
D . High FREQUENCY DIELECTRIC CONSTANTS OF PROTEIN SOLUTIONS
The dielectric constants of protein solutions are slightly lower than that of water at
very high frequencies . This is because protein molecules behave like nonpolar ...
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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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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