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 115
... absorption in the 190 mμ region cannot now be carried out , a change in absorption at 190 mu can still be used as a measure of conformational change . A large part of the absorption change observed at 190 mu may be produced by changes ...
... absorption in the 190 mμ region cannot now be carried out , a change in absorption at 190 mu can still be used as a measure of conformational change . A large part of the absorption change observed at 190 mu may be produced by changes ...
Page 123
... absorption coefficient was concentra- tion - independent ; ( 3 ) solvent perturbation experiments using methanol , ethylene glycol , polyethylene glycol , and glycerol ( Herskovits and Laskowski , 1962b ) and D2O ( Donovan , 1967a ) ...
... absorption coefficient was concentra- tion - independent ; ( 3 ) solvent perturbation experiments using methanol , ethylene glycol , polyethylene glycol , and glycerol ( Herskovits and Laskowski , 1962b ) and D2O ( Donovan , 1967a ) ...
Page 139
... absorption near 230 mμ than near 280 mp . Some of this change in absorption may be produced by changes in the n → * absorption of the amide bonds in the protein , either because of a change in their geometrical arrangement ( Fig . 2 ) ...
... absorption near 230 mμ than near 280 mp . Some of this change in absorption may be produced by changes in the n → * absorption of the amide bonds in the protein , either because of a change in their geometrical arrangement ( Fig . 2 ) ...
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