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 408
... concentration ( see theoretical patterns presented in Figs . 7 and 8 of Cann and Goad , 1965a ) , ( 2 ) the observed changes in pH across the several peaks in the patterns , ( 3 ) the depend- ence of the electrophoretic patterns upon ...
... concentration ( see theoretical patterns presented in Figs . 7 and 8 of Cann and Goad , 1965a ) , ( 2 ) the observed changes in pH across the several peaks in the patterns , ( 3 ) the depend- ence of the electrophoretic patterns upon ...
Page 473
... concentration limit for which gel filtration data may be obtained , in order to facilitate extrapolation of M to zero solute concentration . This method of monomer molecular weight estimation has been demon- strated with a ...
... concentration limit for which gel filtration data may be obtained , in order to facilitate extrapolation of M to zero solute concentration . This method of monomer molecular weight estimation has been demon- strated with a ...
Page 475
... concentration dependence of migration rate ( Winzor and Nichol , 1965 ) . Consequently , estimates of solute purity require analyses whereby effects of concentration dependence may be either taken into account or neglected . A ...
... concentration dependence of migration rate ( Winzor and Nichol , 1965 ) . Consequently , estimates of solute purity require analyses whereby effects of concentration dependence may be either taken into account or neglected . A ...
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