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 7
... intensity . In the electron microscope , absorption of electrons is , and in fact must be , of negligible importance , since appreciable absorption of elec- trons by the specimen would lead rapidly to its thermal destruction ...
... intensity . In the electron microscope , absorption of electrons is , and in fact must be , of negligible importance , since appreciable absorption of elec- trons by the specimen would lead rapidly to its thermal destruction ...
Page 172
... intensity of emitted radiation ( in terms of quanta emitted in unit time ) probability of spontaneous transition number of excited molecules at equilibrium " natural " lifetime of the excited state in the absence of perturbations ...
... intensity of emitted radiation ( in terms of quanta emitted in unit time ) probability of spontaneous transition number of excited molecules at equilibrium " natural " lifetime of the excited state in the absence of perturbations ...
Page 189
... Intensity While the intensity of fluorescence of a sample can be measured ex- actly , for many purposes it is sufficient merely to obtain a quantity , the " observed fluorescence intensity , " expressed in arbitrary detector units . For ...
... Intensity While the intensity of fluorescence of a sample can be measured ex- actly , for many purposes it is sufficient merely to obtain a quantity , the " observed fluorescence intensity , " expressed in arbitrary detector units . For ...
Contents
Electron Microscopy of Globular Proteins | 2 |
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Copyright | |
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absorption absorption spectrum amino acids applied axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann Chem chromophores coefficient components concentration conformational changes contrast curve Debye 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 energy enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups intensity interactions ionic strength ionization ions light macromolecules measured method migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole perturbation phase phenolic Phys plot polarization polymer produced protein proton quantum yield ratio reaction relaxation residues resolution ribonuclease shown in Fig solution solvent specimen spectra structure technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone