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 148
... Tryptophan Since tryptophan is destroyed during the acid hydrolysis used in pre- paring samples for amino acid analysis , it is more convenient to deter- mine the tryptophan content from the ultraviolet absorption of the intact protein ...
... Tryptophan Since tryptophan is destroyed during the acid hydrolysis used in pre- paring samples for amino acid analysis , it is more convenient to deter- mine the tryptophan content from the ultraviolet absorption of the intact protein ...
Page 224
... tryptophan are characteristic of tyrosine , whereas when tryptophan is also present they resemble that of tryptophan even when the major part of the exciting radiation is absorbed by tyrosine ( Teale , 1960 ) . It is possible to resolve ...
... tryptophan are characteristic of tyrosine , whereas when tryptophan is also present they resemble that of tryptophan even when the major part of the exciting radiation is absorbed by tyrosine ( Teale , 1960 ) . It is possible to resolve ...
Page 225
... tryptophan and tyrosine as n increases ( Edelhoch et al . , 1967 ) . The quantum yield of free tryptophan decreases by 50 % and that of tyrosine by 20 % between 25 ° and 50 ° C ( Gally and Edelman , 1964 ) . Proteins which are stable in ...
... tryptophan and tyrosine as n increases ( Edelhoch et al . , 1967 ) . The quantum yield of free tryptophan decreases by 50 % and that of tyrosine by 20 % between 25 ° and 50 ° C ( Gally and Edelman , 1964 ) . Proteins which are stable in ...
Contents
Electron Microscopy of Globular Proteins | 2 |
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
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 conformational changes 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 elution volume emission energy enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups 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 Phys plot polarization polymer produced protein proton quantum yield ratio reaction relaxation residues resolution ribonuclease shown in Fig solution solvent specimen spectra structure technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone