Physical Principles and Techniques of Protein ChemistryPhysical Principles and Techniques of Protein Chemistry Part C ... |
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Page 81
... factors may be found by a process termed least - squares refinement in which
the various parameters are adjusted simultaneously to reduce the discrepancy
between the observed and calculated structure amplitudes to a minimum . As
each ...
... factors may be found by a process termed least - squares refinement in which
the various parameters are adjusted simultaneously to reduce the discrepancy
between the observed and calculated structure amplitudes to a minimum . As
each ...
Page 132
Often , the degree of chromophore exposure calculated from the absorption
change produced by the glycol added to the protein solution containing the
preferentially solvating perturbant will not agree with TABLE IX PERTURBATION
OF ...
Often , the degree of chromophore exposure calculated from the absorption
change produced by the glycol added to the protein solution containing the
preferentially solvating perturbant will not agree with TABLE IX PERTURBATION
OF ...
Page 300
Mū ( 29 ) The parameter g must be calculated using the statistical mechanics of
liquids . The value of the g parameter indicates the orientation of each molecule
relative to its neighboring molecules . Positive deviations of g from unity mean
that ...
Mū ( 29 ) The parameter g must be calculated using the statistical mechanics of
liquids . The value of the g parameter indicates the orientation of each molecule
relative to its neighboring molecules . Positive deviations of g from unity mean
that ...
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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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Common terms and phrases
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