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 127
... appears to be an inductive increase in electron density at the chromophore , since varia- tion of ionic strength does not appear to affect the absorption . Both the carboxyl and amino groups are attached to the same a - carbon atom , to ...
... appears to be an inductive increase in electron density at the chromophore , since varia- tion of ionic strength does not appear to affect the absorption . Both the carboxyl and amino groups are attached to the same a - carbon atom , to ...
Page 233
... appears to cut the strands leaving the globular subspecies largely intact ( Mihalyi and Godfrey , 1963 ) . The polarization results can be understood if the latter units are loosely joined in the native molecule and their rotational ...
... appears to cut the strands leaving the globular subspecies largely intact ( Mihalyi and Godfrey , 1963 ) . The polarization results can be understood if the latter units are loosely joined in the native molecule and their rotational ...
Page 235
... appears to be one which is char- acterized by a maximum number of intramolecular interactions . The X - ray analysis of the structures of myoglobulin and lysozyme reveal essentially no holes or occluded solvent molecules . The most ...
... appears to be one which is char- acterized by a maximum number of intramolecular interactions . The X - ray analysis of the structures of myoglobulin and lysozyme reveal essentially no holes or occluded solvent molecules . The most ...
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