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 mu region cannot now be carried out , a change in absorption at 190 mμ can still be used as a measure of conformational change . A large part of the absorption change observed at 190 mμ may be produced by changes ...
... absorption in the 190 mu region cannot now be carried out , a change in absorption at 190 mμ can still be used as a measure of conformational change . A large part of the absorption change observed at 190 mμ 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 mu . 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 mu . 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 | 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