Physical Principles and Techniques of Protein Chemistry, Part 1 |
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Page 127
pH, a titration curve of the amino acid is obtained, in which the maximum change
in Ae as a function of pH occurs at the pH values corresponding to the pK' of the a
-carboxyl and a-amino groups. The change in absorption for each dissociation ...
pH, a titration curve of the amino acid is obtained, in which the maximum change
in Ae as a function of pH occurs at the pH values corresponding to the pK' of the a
-carboxyl and a-amino groups. The change in absorption for each dissociation ...
Page 145
120 for each of three exposed groups. The wavelength shift produced by this
perturbant can be calculated using Eq. (12). The maximum slope at the long
wavelength end of the spectrum of acetyltyrosine ethyl ester is —200 + 10e/mp at
285.0 ...
120 for each of three exposed groups. The wavelength shift produced by this
perturbant can be calculated using Eq. (12). The maximum slope at the long
wavelength end of the spectrum of acetyltyrosine ethyl ester is —200 + 10e/mp at
285.0 ...
Page 146
Sydney J. Leach. F. REPORTER GROUPs Although most proteins contain a
large number of chromophores, it may be that none of these chromophores is
located in or near a region which is important to the biological function of the
protein.
Sydney J. Leach. F. REPORTER GROUPs Although most proteins contain a
large number of chromophores, it may be that none of these chromophores is
located in or near a region which is important to the biological function of the
protein.
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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