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 2
... resolution at the level of the guaranteed resolv- ing power can be obtained only during the observation of specimens of high contrast in which spacings of appropriate dimensions are present . With instruments currently available , ...
... resolution at the level of the guaranteed resolv- ing power can be obtained only during the observation of specimens of high contrast in which spacings of appropriate dimensions are present . With instruments currently available , ...
Page 20
... resolution objective lenses , however , symmetry is very critical . Symmetry may be disturbed by slight scratching or other mechanical damage , by small fluffs or threads which may catch on the lens surface , or by the asymmetric ...
... resolution objective lenses , however , symmetry is very critical . Symmetry may be disturbed by slight scratching or other mechanical damage , by small fluffs or threads which may catch on the lens surface , or by the asymmetric ...
Page 26
... Resolution in Shadow - Cast Preparations The limitations of the shadowing method for specimen contrast en- hancement include the fact that only surface structure is revealed by the technique , and more important , that features of the ...
... Resolution in Shadow - Cast Preparations The limitations of the shadowing method for specimen contrast en- hancement include the fact that only surface structure is revealed by the technique , and more important , that features of the ...
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