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 199
... given excitation wavelength λ is given by F ( x ) = K dq / dλ × E ( x ) ( 37 ) where Kdq / dλ is the fluorescence in relative quanta and E ( X ) is the relative photon output of the excitation system at that wavelength . Cali- bration ...
... given excitation wavelength λ is given by F ( x ) = K dq / dλ × E ( x ) ( 37 ) where Kdq / dλ is the fluorescence in relative quanta and E ( X ) is the relative photon output of the excitation system at that wavelength . Cali- bration ...
Page 374
... given by the relation μ = E - 1 dx Q dt f = = QD kT ( 5 ) If the particle is a sphere of radius a , the frictional coefficient is given by Stokes ' law as 67ŋa , where is the coefficient of viscosity of the solvent medium . The radius ...
... given by the relation μ = E - 1 dx Q dt f = = QD kT ( 5 ) If the particle is a sphere of radius a , the frictional coefficient is given by Stokes ' law as 67ŋa , where is the coefficient of viscosity of the solvent medium . The radius ...
Page 387
... given component is equal to the ratio of the area under its peak to the total area exclusive of that due to the and 8 boundary . This relation assumes , of course , that the various components all have the same refractive increment ...
... given component is equal to the ratio of the area under its peak to the total area exclusive of that due to the and 8 boundary . This relation assumes , of course , that the various components all have the same refractive increment ...
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