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 9
... phase interference between co- incident rays which differ in optical path length . The effect is an ex- ample of phase contrast - as opposed to the amplitude contrast which results from the absorption or scattering of light or electrons ...
... phase interference between co- incident rays which differ in optical path length . The effect is an ex- ample of phase contrast - as opposed to the amplitude contrast which results from the absorption or scattering of light or electrons ...
Page 211
... phase photometry , a fluorescent sample is irradiated by a modulated light beam and the phase shift produced as a consequence of the finite duration of the excited state is measured ( Pringsheim , 1949 ; Steiner and McAlister , 1957a ...
... phase photometry , a fluorescent sample is irradiated by a modulated light beam and the phase shift produced as a consequence of the finite duration of the excited state is measured ( Pringsheim , 1949 ; Steiner and McAlister , 1957a ...
Page 212
... phase until the two coupled outputs exhibit maximum interference ( i.e. , are completely out of phase ) . This produces a minimum net signal . The usual procedure is to perform the null balancing first with a scattering suspension ...
... phase until the two coupled outputs exhibit maximum interference ( i.e. , are completely out of phase ) . This produces a minimum net signal . The usual procedure is to perform the null balancing first with a scattering suspension ...
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