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 134
... disulfide bond , and another tyrosyl residue is only one residue removed from a disulfide bond , perturbants probably have limited access to these residues in the unfolded but unreduced protein . Ribo- nuclease undergoes a ...
... disulfide bond , and another tyrosyl residue is only one residue removed from a disulfide bond , perturbants probably have limited access to these residues in the unfolded but unreduced protein . Ribo- nuclease undergoes a ...
Page 166
... disulfide bond . Because of repulsion between 3p orbitals of the sulfur atoms , the disulfide chromophore has a dihedral angle of 90 ° in the unstrained condition . Since two nonsuper- posable forms can be constructed , and because the ...
... disulfide bond . Because of repulsion between 3p orbitals of the sulfur atoms , the disulfide chromophore has a dihedral angle of 90 ° in the unstrained condition . Since two nonsuper- posable forms can be constructed , and because the ...
Page 235
... disulfide bonds , which produced only small , instantaneous effects on viscosity and optical rotation . Only in 6 M guanidine solutions were the polarization values comparable with those reported for homologous polypeptides in their ...
... disulfide bonds , which produced only small , instantaneous effects on viscosity and optical rotation . Only in 6 M guanidine solutions were the polarization values comparable with those reported for homologous polypeptides in their ...
Contents
Electron Microscopy | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorbance absorption change absorption spectrum amino acids angle axis 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