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 109
... chromophores , it is necessary to consider in detail the effect of solvents . on chromophores . Solvents alter the intensity of absorption of a chromophore and shift its absorption spectrum along the wavelength scale . The change is de ...
... chromophores , it is necessary to consider in detail the effect of solvents . on chromophores . Solvents alter the intensity of absorption of a chromophore and shift its absorption spectrum along the wavelength scale . The change is de ...
Page 130
... chromophores exposed to water at the surface of a protein molecule are " red - shifted " relative to the vapor spectrum , be- cause of the polarization red shift described above ( Section II , B ) . By changing the composition of the ...
... chromophores exposed to water at the surface of a protein molecule are " red - shifted " relative to the vapor spectrum , be- cause of the polarization red shift described above ( Section II , B ) . By changing the composition of the ...
Page 138
... chromophores exposed to the solvent in the native protein ( from the initial rate of change of absorption with perturbant concentration ) and the number of chromophores released to the solvent in the denaturation process ( from the ...
... chromophores exposed to the solvent in the native protein ( from the initial rate of change of absorption with perturbant concentration ) and the number of chromophores released to the solvent in the denaturation process ( from the ...
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