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 52
... molecules in solution . At best , about half of the molecules are seen to have undergone some degree of denaturation . That a molecule so thoroughly characterized as that of bovine serum albumin should be found to be extensively dam ...
... molecules in solution . At best , about half of the molecules are seen to have undergone some degree of denaturation . That a molecule so thoroughly characterized as that of bovine serum albumin should be found to be extensively dam ...
Page 238
... molecules bound remains constant . At pH 5.0 a highly cooperative bind- ing of the five dye molecules occurs , while at pH 7.0 the binding curve is normal except that the affinity for the first molecule is much greater than for the rest ...
... molecules bound remains constant . At pH 5.0 a highly cooperative bind- ing of the five dye molecules occurs , while at pH 7.0 the binding curve is normal except that the affinity for the first molecule is much greater than for the rest ...
Page 304
... molecular rotation is restricted by molecular interactions . Due to local fluctuations in the interaction energy , the potential energy which restricts the free orienta- tion of individual molecules is not necessarily uniform throughout ...
... molecular rotation is restricted by molecular interactions . Due to local fluctuations in the interaction energy , the potential energy which restricts the free orienta- tion of individual molecules is not necessarily uniform throughout ...
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