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 137
... Extrapolation of the straight - line portion of the curve to zero concentration of GCl gives the Ae for transfer of the buried phenolic chromophores from the interior of ribonuclease into water , since the extrapolation procedure ...
... Extrapolation of the straight - line portion of the curve to zero concentration of GCl gives the Ae for transfer of the buried phenolic chromophores from the interior of ribonuclease into water , since the extrapolation procedure ...
Page 343
... extrapolation methods , for example , by extrapolating a An vs. 1 / E2 plot to E∞ . In this way the optical anisotropy factor is determined . Holcomb and Tinoco ( 1963 ) made calculations of the electric bire- fringence at high field ...
... extrapolation methods , for example , by extrapolating a An vs. 1 / E2 plot to E∞ . In this way the optical anisotropy factor is determined . Holcomb and Tinoco ( 1963 ) made calculations of the electric bire- fringence at high field ...
Page 393
... Extrapolation of apparent electrophoretic analysis at various protein concentrations and salt concentrations to " ideal conditions " ( Alberty , 1948a ) : % P - protein concentration ( % by weight ) , T = ionic strength ...
... Extrapolation of apparent electrophoretic analysis at various protein concentrations and salt concentrations to " ideal conditions " ( Alberty , 1948a ) : % P - protein concentration ( % by weight ) , T = ionic strength ...
Contents
Electron Microscopy of Globular Proteins | 2 |
Operational Requirements for HighResolution Electron | 15 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorbance absorption change absorption spectrum amino acids applied atoms axis binding Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann carboxyl cell Chem chromophores coefficient components conformational changes curve Debye denaturation determined dielectric constant dielectric increment dielectric relaxation difference spectrum dipole moment Edelhoch effects electric birefringence electric field electron electrophoresis elution volume emission energy enzyme equation equilibrium excitation experimental fluorescence fraction frequency gel filtration glycol gradient intensity interactions ionic strength ionization ions light linear macromolecules measured method migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole phenolic phenolic groups phenylalanine photomultiplier Phys plot polarization polymer produced proton quantum yield ratio reaction relaxation residues ribonuclease rotational diffusion sample shift shown in Fig solvent spectra spectrofluorometer structure technique temperature theoretical theory tion transition tryptophan tyrosine tyrosyl ultraviolet values wavelength Weber Winzor zone