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 78
... effect in L - alanine is given by Marsh and Donohue ( 1967 ) . The effect of disorder on a Fourier synthesis is illustrated in Fig . 13 and it will be seen that an increase in B leads to a reduction in the effective resolution . In ...
... effect in L - alanine is given by Marsh and Donohue ( 1967 ) . The effect of disorder on a Fourier synthesis is illustrated in Fig . 13 and it will be seen that an increase in B leads to a reduction in the effective resolution . In ...
Page 127
... effects would then take the same path from the a - carbon atom . In agree- ment with this hypothesis , the ratio of the effect of deprotonation of the carboxyl group to the effect of deprotonation of the NH3 + group appears to be ...
... effects would then take the same path from the a - carbon atom . In agree- ment with this hypothesis , the ratio of the effect of deprotonation of the carboxyl group to the effect of deprotonation of the NH3 + group appears to be ...
Page 128
... effect mediated by the solvent proper and therefore affected by ionic strength . ( 5 ) An inductive effect through the covalent bonds of the protein . ( 6 ) An alteration in the water struc- ture ( electrostrictive changes ) near the ...
... effect mediated by the solvent proper and therefore affected by ionic strength . ( 5 ) An inductive effect through the covalent bonds of the protein . ( 6 ) An alteration in the water struc- ture ( electrostrictive changes ) near the ...
Contents
Electron Microscopy | 2 |
Ultraviolet Absorption | 3 |
Operational Requirements for HighResolution Electron | 15 |
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absorbance absorption change absorption spectrum amino acids angle axis binding Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Chem chromophores coefficient concentration conformational changes contrast curve denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction dipole moment Edelhoch effect electric birefringence electric field electron microscope electrophoresis elution emission energy equation equilibrium excitation experimental factor film fluorescence frequency function gel filtration glycol instrument intensity interactions ionic strength ionization ions light macromolecules measured method mobility molar molecular weight molecules moving-boundary observed obtained optical parameter particles patterns peaks permanent dipole phase phenolic phenolic groups phenylalanine photomultiplier Phys polarization produced protein proton quantum yield ratio reaction relaxation residues ribonuclease rotational diffusion sample scattering shift shown in Fig solution solvent specimen spectra spectrofluorometer structure technique temperature theory tion tryptophan tyrosine ultraviolet unit cell values wavelength Weber zone