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 323
... gradient is still re- quired to orient the molecule appreciably . The shear gradient used by Jacobsen and Wenner does not seem to have been sufficient to orient the molecules appreciably and hemocyanin molecules were probably randomly ...
... gradient is still re- quired to orient the molecule appreciably . The shear gradient used by Jacobsen and Wenner does not seem to have been sufficient to orient the molecules appreciably and hemocyanin molecules were probably randomly ...
Page 409
... gradient of protein concen- tration between the two ascending peaks . Eventually , however , this gradient is obliterated by mild convection . Very small convective " pips " sometimes develop along the trailing edge of the fast peak and ...
... gradient of protein concen- tration between the two ascending peaks . Eventually , however , this gradient is obliterated by mild convection . Very small convective " pips " sometimes develop along the trailing edge of the fast peak and ...
Page 432
... gradient of sucrose or D2O than by moving - boundary electrophoresis . Zone electrophoresis in a den- sity gradient also holds promise as a powerful tool for quantitative characterization of certain macromolecular interactions such as ...
... gradient of sucrose or D2O than by moving - boundary electrophoresis . Zone electrophoresis in a den- sity gradient also holds promise as a powerful tool for quantitative characterization of certain macromolecular interactions such as ...
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