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 129
... perturbed , since they are not isolated as they are in the vapor phase , but they are perturbed to different extents . The solvent perturbation technique was introduced by Herskovits and Laskowski ( 1960 ) . In this procedure ...
... perturbed , since they are not isolated as they are in the vapor phase , but they are perturbed to different extents . The solvent perturbation technique was introduced by Herskovits and Laskowski ( 1960 ) . In this procedure ...
Page 130
... perturbation experiment must be " calibrated " in order to interpret the observed absorption change in terms of the number of chromophores exposed to the solvent . One method of measuring the solvent perturbation of all the chromophores ...
... perturbation experiment must be " calibrated " in order to interpret the observed absorption change in terms of the number of chromophores exposed to the solvent . One method of measuring the solvent perturbation of all the chromophores ...
Page 166
... perturbed , but also the nature of the perturbation . Molecular geometry , an important determinant for the absorption of protein amide bonds , has been ignored in studies of perturbations of the chromophores of proteins . It seems very ...
... perturbed , but also the nature of the perturbation . Molecular geometry , an important determinant for the absorption of protein amide bonds , has been ignored in studies of perturbations of the chromophores of proteins . It seems very ...
Contents
SLAYTER | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorption absorption spectrum amino acids applied axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann Chem chromophores coefficient components concentration contrast curve Debye denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction dipole moment Edelhoch effects electric birefringence electric field electron microscope electrophoresis electrophoretic patterns elution volume emission energy enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups heavy atom intensity interactions ionic strength ionization ions light macromolecules measured method 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 protein proton quantum yield ratio reaction relaxation residues resolution ribonuclease shadow shown in Fig solution solvent specimen spectra structure technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone