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
... contrast must be considered in interpretating a microscope image . In the ordinary light microscope , contrast is achieved principally because of differences in the extent of absorption of light between different parts of the specimen ...
... contrast must be considered in interpretating a microscope image . In the ordinary light microscope , contrast is achieved principally because of differences in the extent of absorption of light between different parts of the specimen ...
Page 9
... contrast of specimens of low average atomic number can be enhanced instrumentally by the use of a limiting objective aper- ture . The aperture of the objective lenses of electron microscopes is somewhat larger in practice than the ...
... contrast of specimens of low average atomic number can be enhanced instrumentally by the use of a limiting objective aper- ture . The aperture of the objective lenses of electron microscopes is somewhat larger in practice than the ...
Page 31
... contrast . Six types of virus ( vaccinia , influenza , herpes , adenovirus , polyoma , and polio ) each ap- peared at least somewhat larger by negative contrast than in sections . Structural differences , as observed at high resolution ...
... contrast . Six types of virus ( vaccinia , influenza , herpes , adenovirus , polyoma , and polio ) each ap- peared at least somewhat larger by negative contrast than in sections . Structural differences , as observed at high resolution ...
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