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 166
... studies of perturbations of the chromophores of proteins . It seems very likely that the geometrical relation ... Studies of the absorption , optical rotation and circular dichroism of disulfide bonds in proteins and model compounds will ...
... studies of perturbations of the chromophores of proteins . It seems very likely that the geometrical relation ... Studies of the absorption , optical rotation and circular dichroism of disulfide bonds in proteins and model compounds will ...
Page 474
... studies at even lower concentrations by the frontal gel filtration technique clearly demonstrate the breakdown of tetramer ( Fig . 7 ) , dissociation of which is essentially complete at the concentrations used for enzymic assay ...
... studies at even lower concentrations by the frontal gel filtration technique clearly demonstrate the breakdown of tetramer ( Fig . 7 ) , dissociation of which is essentially complete at the concentrations used for enzymic assay ...
Page 480
... Studies of Rapid Chemical Equilibria In studies of interacting protein systems by gel filtration the effects of the chemical reaction upon the elution profiles vary according to the equilibrium position and the rate of re ...
... Studies of Rapid Chemical Equilibria In studies of interacting protein systems by gel filtration the effects of the chemical reaction upon the elution profiles vary according to the equilibrium position and the rate of re ...
Contents
Electron Microscopy of Globular Proteins | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorption absorption spectrum applied atoms axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann Chem chromophores coefficient components concentration curve denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction dipole moment Edelhoch effects electric birefringence electric field electron microscope electrophoresis elution volume emission enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups intensity interactions ionic strength ions lens light linear macromolecules measured method micrographs migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole perturbation phase phenolic photomultiplier Phys plot polarization polymer produced protein quantum yield ratio reaction relaxation residues resolution resolving power ribonuclease scattering shadow shown in Fig solution solvent specimen spectra structure studies technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone