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 initial ...
... 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 initial ...
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 250
... temperature - jump experiment . Instantaneous concentration [ S , 1 . Equilibrium con- centration [ 5 , ] . The time course of the temperature follows the curve for S ;. ( b ) The interaction of a - chymotrypsin with acridine orange ...
... temperature - jump experiment . Instantaneous concentration [ S , 1 . Equilibrium con- centration [ 5 , ] . The time course of the temperature follows the curve for S ;. ( b ) The interaction of a - chymotrypsin with acridine orange ...
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