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 131
... conformational changes in most proteins studied under reasonable conditions of pH , ionic strength , and temperature . Conformational changes can be suspected if the perturbation is found to be nonlinear with respect to perturbant ...
... conformational changes in most proteins studied under reasonable conditions of pH , ionic strength , and temperature . Conformational changes can be suspected if the perturbation is found to be nonlinear with respect to perturbant ...
Page 146
... conformational change , or on a surface at which association takes place , then an artificial chromophore may be inserted by chemical modification of the protein . Such a chromophore has been termed a " reporter group " ( Burr and ...
... conformational change , or on a surface at which association takes place , then an artificial chromophore may be inserted by chemical modification of the protein . Such a chromophore has been termed a " reporter group " ( Burr and ...
Page 226
... conformational changes in proteins . The optical methods of rotatory dispersion , circular dichroism , difference spectra , and fluorescence meas- urements offer many advantages in terms of sensitivity , specificity , and kinetic ...
... conformational changes in proteins . The optical methods of rotatory dispersion , circular dichroism , difference spectra , and fluorescence meas- urements offer many advantages in terms of sensitivity , specificity , and kinetic ...
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