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 ... |
From inside the book
Results 1-3 of 58
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 | 2 |
Ultraviolet Absorption | 3 |
Operational Requirements for HighResolution Electron | 15 |
Copyright | |
66 other sections not shown
Other editions - View all
Common terms and phrases
absorbance absorption change absorption spectrum amino acids angle axis binding 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