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 157
... solutions having equal increments in con- centration is used . They are measured one against another , in such a way that the concentration difference between the sample solution and the reference solution is always constant . A plot of ...
... solutions having equal increments in con- centration is used . They are measured one against another , in such a way that the concentration difference between the sample solution and the reference solution is always constant . A plot of ...
Page 160
... solution can often be conveniently altered by adding concentrated acid or base solution to the sample solution using a syringe microburet or a glass rod drawn to a fine tip . Except at ex- tremes of pH , the volume change so produced is ...
... solution can often be conveniently altered by adding concentrated acid or base solution to the sample solution using a syringe microburet or a glass rod drawn to a fine tip . Except at ex- tremes of pH , the volume change so produced is ...
Page 161
... Solutions For convenience , the reference solution for spectrophotometric titra- tions should have all the titratable chromophores in one absorbing form ( see Section IV ) . For titrations of phenolic groups , a neutral pH reference ...
... Solutions For convenience , the reference solution for spectrophotometric titra- tions should have all the titratable chromophores in one absorbing form ( see Section IV ) . For titrations of phenolic groups , a neutral pH reference ...
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