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 418
... complex and , in fact , its area proved to be an empirical index of the extent of binding of serum albumin by pepsin . Several independent lines of evidence were presented suggesting that this complex is the spe- cific Michaelis ...
... complex and , in fact , its area proved to be an empirical index of the extent of binding of serum albumin by pepsin . Several independent lines of evidence were presented suggesting that this complex is the spe- cific Michaelis ...
Page 419
... complex between a proteolytic enzyme and its macromolecular substrate . Previously , the existence of the Michaelis- Menten complex had been shown only for low molecular weight sub- strates ( Chance , 1943 , 1951 ; Doherty and Vaslow ...
... complex between a proteolytic enzyme and its macromolecular substrate . Previously , the existence of the Michaelis- Menten complex had been shown only for low molecular weight sub- strates ( Chance , 1943 , 1951 ; Doherty and Vaslow ...
Page 421
... complex than that . Thus , a single macro- molecule which isomerizes reversibly at rates comparable to the rate of electrophoretic separation of the isomers can give three zones . Furthermore , conclusions concerning the molecular forms ...
... complex than that . Thus , a single macro- molecule which isomerizes reversibly at rates comparable to the rate of electrophoretic separation of the isomers can give three zones . Furthermore , conclusions concerning the molecular forms ...
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