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 26
... technique , and more important , that features of the specimen smaller than a certain size are concealed by accumulated metal . It is found that under optimum conditions of evaporation , individual globular particles down to 40 or 50 Å ...
... technique , and more important , that features of the specimen smaller than a certain size are concealed by accumulated metal . It is found that under optimum conditions of evaporation , individual globular particles down to 40 or 50 Å ...
Page 275
... technique because so far this has been the most valuable and accessible of the chemical relaxation techniques in biochemical research . Many of the principles which have been discussed here are applicable to other per- turbation methods ...
... technique because so far this has been the most valuable and accessible of the chemical relaxation techniques in biochemical research . Many of the principles which have been discussed here are applicable to other per- turbation methods ...
Page 474
... technique clearly demonstrate the breakdown of tetramer ( Fig . 7 ) , dissociation of which is essentially complete at the concentrations used for enzymic assay ( < 0.0003 mg / ml ) . Provided the presence of sub- strate does not affect ...
... technique clearly demonstrate the breakdown of tetramer ( Fig . 7 ) , dissociation of which is essentially complete at the concentrations used for enzymic assay ( < 0.0003 mg / ml ) . Provided the presence of sub- strate does not affect ...
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