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 166
... important determinant for the absorption of protein amide bonds , has been ignored in studies of perturbations of the chromophores of proteins . It seems very likely that the geometrical relation between the chromophore and a perturbant ...
... important determinant for the absorption of protein amide bonds , has been ignored in studies of perturbations of the chromophores of proteins . It seems very likely that the geometrical relation between the chromophore and a perturbant ...
Page 220
... important contribution to the low yield at neutral pH may be proton transfer from the excited tyrosyl to charged carboxylate side chains , since small molecules containing carboxylate groups are efficient quenchers of phenol ...
... important contribution to the low yield at neutral pH may be proton transfer from the excited tyrosyl to charged carboxylate side chains , since small molecules containing carboxylate groups are efficient quenchers of phenol ...
Page 424
... important difficulty arises from the superposition of electro- osmotic transport of the solution as a whole upon electrophoretic migra- tion . Migration is observed relative to the supporting medium , whereas the mobility must be ...
... important difficulty arises from the superposition of electro- osmotic transport of the solution as a whole upon electrophoretic migra- tion . Migration is observed relative to the supporting medium , whereas the mobility must be ...
Contents
Electron Microscopy of Globular Proteins | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorption absorption spectrum applied atoms axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann Chem chromophores coefficient components concentration curve 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 enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups intensity interactions ionic strength ions lens light linear macromolecules measured method micrographs migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole perturbation phase phenolic photomultiplier Phys plot polarization polymer produced protein quantum yield ratio reaction relaxation residues resolution resolving power ribonuclease scattering shadow shown in Fig solution solvent specimen spectra structure studies technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone