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 304
... RELAXATION TIMES In the discussion presented hitherto , it is tacitly assumed that the dielectric relaxation is characterized by only one relaxation time . The theory described above is therefore referred to as the Debye theory ...
... RELAXATION TIMES In the discussion presented hitherto , it is tacitly assumed that the dielectric relaxation is characterized by only one relaxation time . The theory described above is therefore referred to as the Debye theory ...
Page 320
... relaxation in the neighborhood of 20 kc and would not contribute any dielectric increment in the 1 mc region . Takashima and Schwan ( 1959 ) investigated the dielectric constant of ovalbumin between 100 cps and 200 kc but no additional ...
... relaxation in the neighborhood of 20 kc and would not contribute any dielectric increment in the 1 mc region . Takashima and Schwan ( 1959 ) investigated the dielectric constant of ovalbumin between 100 cps and 200 kc but no additional ...
Page 321
... relaxation time should be proportional to the viscosity of the solvent . Takashima ( 1962 ) Relaxation time ( 10-6 sec ) 1.5 1.0 0.5- 2.0 T O a b 3 5 7 9 Viscocity ( centipoise ) FIG . 10. Dependence of the relaxation time of proteins ...
... relaxation time should be proportional to the viscosity of the solvent . Takashima ( 1962 ) Relaxation time ( 10-6 sec ) 1.5 1.0 0.5- 2.0 T O a b 3 5 7 9 Viscocity ( centipoise ) FIG . 10. Dependence of the relaxation time of proteins ...
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