Physical Principles and Techniques of Protein ChemistryPhysical Principles and Techniques of Protein Chemistry Part C ... |
From inside the book
Results 1-3 of 78
Page 235
Unfolded States The native state of globular proteins appears to be one which is
characterized by a maximum number of intramolecular interactions . The X - ray
analysis of the structures of myoglobulin and lysozyme reveal essentially no ...
Unfolded States The native state of globular proteins appears to be one which is
characterized by a maximum number of intramolecular interactions . The X - ray
analysis of the structures of myoglobulin and lysozyme reveal essentially no ...
Page 439
Aside from fundamental investigations on protein interactions per se , it is
obviously desirable to avoid conditions conducive to the production of
electrophoretic patterns which do not faithfully reflect the inherent state of
homogeneity of the ...
Aside from fundamental investigations on protein interactions per se , it is
obviously desirable to avoid conditions conducive to the production of
electrophoretic patterns which do not faithfully reflect the inherent state of
homogeneity of the ...
Page 493
The former advantage would facilitate the determination of equilibrium data on
interactions involving unstable proteins such as the proteolytic enzymes , while
the latter would prove useful in the study of rapid equilibria involving proteins and
...
The former advantage would facilitate the determination of equilibrium data on
interactions involving unstable proteins such as the proteolytic enzymes , while
the latter would prove useful in the study of rapid equilibria involving proteins and
...
What people are saying - Write a review
We haven't found any reviews in the usual places.
Contents
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Examples of the Application of Electron Microscopy to the Study | 48 |
Copyright | |
20 other sections not shown
Other editions - View all
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