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 264
... range . The fast effect was also found at pH 9 in the absence of PF ( CT + buffer ) , whereas PF alone did not give rise to any relaxation effect in the 10 μsec range . Since the reaction only involved CT and could be followed with a ...
... range . The fast effect was also found at pH 9 in the absence of PF ( CT + buffer ) , whereas PF alone did not give rise to any relaxation effect in the 10 μsec range . Since the reaction only involved CT and could be followed with a ...
Page 267
... range 107-108 M - 1 sec - 1 1 , the dissociation rate constant for the complex near 103 sec - 1 , and isomeriza- tion rate constants in the range 10-10 sec - 1 . The equilibrium constant for isomerization of the enzyme- " substrate ...
... range 107-108 M - 1 sec - 1 1 , the dissociation rate constant for the complex near 103 sec - 1 , and isomeriza- tion rate constants in the range 10-10 sec - 1 . The equilibrium constant for isomerization of the enzyme- " substrate ...
Page 270
... range , is ascribed to the bind- ing of L in the R - series . The next effect , occurring in the millisecond range , is assigned to the binding of L in the T - series . In both cases , simple bimolecular kinetics were found . The ...
... range , is ascribed to the bind- ing of L in the R - series . The next effect , occurring in the millisecond range , is assigned to the binding of L in the T - series . In both cases , simple bimolecular kinetics were found . The ...
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