Physical Principles and Techniques of Protein Chemistry, Part 1Sydney J. Leach Physical Principles and Techniques of Protein Chemistry, Part A deals with the principles and application of selected physical methods in protein chemistry evaluation. This book is organized into nine chapters that cover microscopic, crystallographic, and electrophoretic techniques for protein conformational perturbations evaluation. This text first presents a general account of electron microscopy, its specimen preparation, optimum conditions for high resolution, measurement of electron micrographs, and illustrative examples of protein study. This book then examines the different types of map ... |
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Page 375
... ionic atmosphere of opposite charge . The presence of the ionic atmosphere results in electrophoretic mobilities which are smaller than those predicted by Eqs . ( 5 ) and ( 6 ) . Three factors contribute to this difference . First , the ...
... ionic atmosphere of opposite charge . The presence of the ionic atmosphere results in electrophoretic mobilities which are smaller than those predicted by Eqs . ( 5 ) and ( 6 ) . Three factors contribute to this difference . First , the ...
Page 391
... ionic species that may be present . Consequently , the change in refractive index across the moving boundary , and ... ionic strength 0.1 ) and a total protein concentration of 2.67 % . He found overall changes in conductance of the ...
... ionic species that may be present . Consequently , the change in refractive index across the moving boundary , and ... ionic strength 0.1 ) and a total protein concentration of 2.67 % . He found overall changes in conductance of the ...
Page 394
... ionic strength on resolution of ovalbumin at pH 6.7 to 6.8 ( Cann , 1949 ) : ( a ) Ionic strength 0.3 . ( b ) Ionic strength 0.1 . ( c ) Ionic strength 0.05 . ment with theoretical prediction , the magnitude of the deviation of apparent ...
... ionic strength on resolution of ovalbumin at pH 6.7 to 6.8 ( Cann , 1949 ) : ( a ) Ionic strength 0.3 . ( b ) Ionic strength 0.1 . ( c ) Ionic strength 0.05 . ment with theoretical prediction , the magnitude of the deviation of apparent ...
Contents
Electron Microscopy | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorbance absorption change absorption spectrum amino acids angle axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Chem chromophores coefficient concentration conformational changes contrast curve denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction dipole moment Edelhoch effect electric birefringence electric field electron microscope electrophoresis elution emission energy equation equilibrium excitation experimental factor film fluorescence frequency function gel filtration glycol instrument intensity interactions ionic strength ionization ions light macromolecules measured method mobility molar molecular weight molecules moving-boundary observed obtained optical parameter particles patterns peaks permanent dipole phase phenolic phenolic groups phenylalanine photomultiplier Phys polarization produced protein proton quantum yield ratio reaction relaxation residues ribonuclease rotational diffusion sample scattering shift shown in Fig solution solvent specimen spectra spectrofluorometer structure technique temperature theory tion tryptophan tyrosine ultraviolet unit cell values wavelength Weber zone