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 264
... dependence of 7. An uncoupled conformational change in the protein should not show any concentration dependence of 7 . Whereas the 10 - μsec effect is far enough from the other on the time scale to be virtually independent , the two ...
... dependence of 7. An uncoupled conformational change in the protein should not show any concentration dependence of 7 . Whereas the 10 - μsec effect is far enough from the other on the time scale to be virtually independent , the two ...
Page 463
... Dependence of Elution Volume Concentration dependence of the elution volume reflects either non- linearity of the partition isotherm for a stable solute , or concentration- dependent changes in the composition of the mobile phase due to ...
... Dependence of Elution Volume Concentration dependence of the elution volume reflects either non- linearity of the partition isotherm for a stable solute , or concentration- dependent changes in the composition of the mobile phase due to ...
Page 475
... 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 comparison of ...
... 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 comparison of ...
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