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 73
... given range of d * may be considerably re- duced by the presence of symmetry . Simplified formulas for each space group are given in the International Tables for X - Ray Crystallography I ( Lonsdale , 1952 ) . A. SECTIONS AND ...
... given range of d * may be considerably re- duced by the presence of symmetry . Simplified formulas for each space group are given in the International Tables for X - Ray Crystallography I ( Lonsdale , 1952 ) . A. SECTIONS AND ...
Page 199
... given excitation wavelength A 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 A 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 389
... given a posi- tive sign if the aß boundary moves with the current and a negative sign if it moves against the current . The current is taken as flowing from the positive to the negative electrode . The concentrations are given a sign ...
... given a posi- tive sign if the aß boundary moves with the current and a negative sign if it moves against the current . The current is taken as flowing from the positive to the negative electrode . The concentrations are given a sign ...
Contents
Electron Microscopy of Globular Proteins | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorption absorption spectrum applied atoms axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann Chem chromophores coefficient components concentration curve 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 enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups intensity interactions ionic strength ions lens light linear macromolecules measured method micrographs migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole perturbation phase phenolic photomultiplier Phys plot polarization polymer produced protein quantum yield ratio reaction relaxation residues resolution resolving power ribonuclease scattering shadow shown in Fig solution solvent specimen spectra structure studies technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone