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 400
... patterns will show two sedimenting peaks despite instantaneous establishment of equilibrium . Likewise , the de- scending ( but not ascending ) moving - boundary electrophoretic pattern will show two peaks provided the electrophoretic ...
... patterns will show two sedimenting peaks despite instantaneous establishment of equilibrium . Likewise , the de- scending ( but not ascending ) moving - boundary electrophoretic pattern will show two peaks provided the electrophoretic ...
Page 405
... patterns ( Cann and Goad , 1965a ) for K1 / n = 101 , n = = 3 and values of C2.0 / C1.0 given below . gradient curves ; pHA . Virtually the same results were obtained for n = 1 , the only differences being quantitative ones . ( a ) C2.0 ...
... patterns ( Cann and Goad , 1965a ) for K1 / n = 101 , n = = 3 and values of C2.0 / C1.0 given below . gradient curves ; pHA . Virtually the same results were obtained for n = 1 , the only differences being quantitative ones . ( a ) C2.0 ...
Page 410
... patterns have also been computed for the other case in which the protein is alkaline to its isoelectric point ( with nega- tive mobilities and the mobility of the complexed protein being smaller than that of the uncomplexed protein ...
... patterns have also been computed for the other case in which the protein is alkaline to its isoelectric point ( with nega- tive mobilities and the mobility of the complexed protein being smaller than that of the uncomplexed protein ...
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