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 139
... produced by the protein interior with the perturbation produced by 20 % ethylene glycol indicates that the interior of a protein is equivalent to 120 % ethylene glycol . Esti- mates of Ae for release of buried chromophores are given in ...
... produced by the protein interior with the perturbation produced by 20 % ethylene glycol indicates that the interior of a protein is equivalent to 120 % ethylene glycol . Esti- mates of Ae for release of buried chromophores are given in ...
Page 141
... produced by ethylene glycol ( Fig . 9 ) . The magnitude ( height ) of the difference spec- trum has the same pH dependence as the activity of the enzyme . When lysozyme is denatured with increasing concentrations of urea , the height ...
... produced by ethylene glycol ( Fig . 9 ) . The magnitude ( height ) of the difference spec- trum has the same pH dependence as the activity of the enzyme . When lysozyme is denatured with increasing concentrations of urea , the height ...
Page 163
... produces a decrease in absorption , the contents of the reference cell are mixed instead . This procedure prevents the recorder pen from going off scale when a nega- tive spectrum is produced . After the perturbation difference spectrum ...
... produces a decrease in absorption , the contents of the reference cell are mixed instead . This procedure prevents the recorder pen from going off scale when a nega- tive spectrum is produced . After the perturbation difference spectrum ...
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