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 140
... temperature , a measure of the amount of denatured protein . present , can be used to determine the equilibrium constant for the de- naturation process at that temperature , provided that the usual thermo- dynamic criteria ( known ...
... temperature , a measure of the amount of denatured protein . present , can be used to determine the equilibrium constant for the de- naturation process at that temperature , provided that the usual thermo- dynamic criteria ( known ...
Page 225
... temperature range show a continuous decrease in fluorescence with increasing temperature . The fluorescence of tryptophan and tyrosine residues which are buried is probably un- affected , or only slightly affected , by temperature ...
... temperature range show a continuous decrease in fluorescence with increasing temperature . The fluorescence of tryptophan and tyrosine residues which are buried is probably un- affected , or only slightly affected , by temperature ...
Page 288
... Temperature - Jump Techniques Some reactions involving proteins are characterized by equilibria which are displaced far over in the direction of the products . In cases where the velocities are too high for measurement by flow methods ...
... Temperature - Jump Techniques Some reactions involving proteins are characterized by equilibria which are displaced far over in the direction of the products . In cases where the velocities are too high for measurement by flow methods ...
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