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 143
... bound to a protein may be useful for determining the number of ions bound , provided that Molar absorption difference ( AE ) +1000 ( e ) ( d ) -1000 BSA dodecylsulfate Ke ) -2000 500 ( f ) O ' Sucrose only • Sucrose in presence of ...
... bound to a protein may be useful for determining the number of ions bound , provided that Molar absorption difference ( AE ) +1000 ( e ) ( d ) -1000 BSA dodecylsulfate Ke ) -2000 500 ( f ) O ' Sucrose only • Sucrose in presence of ...
Page 144
... bound . Thus it appears that the observed blue shift is not produced by an unfolding of the protein which exposes buried chromophores to the solvent . Nor does perturbation of the chromophores by the charges on the bound ions produce ...
... bound . Thus it appears that the observed blue shift is not produced by an unfolding of the protein which exposes buried chromophores to the solvent . Nor does perturbation of the chromophores by the charges on the bound ions produce ...
Page 238
... bound remains constant . At pH 5.0 a highly cooperative bind- ing of the five dye molecules occurs , while at pH 7.0 ... bound to bovine serum albumin for a group of fluorescent dyes by measuring the increase in their polarization . The ...
... bound remains constant . At pH 5.0 a highly cooperative bind- ing of the five dye molecules occurs , while at pH 7.0 ... bound to bovine serum albumin for a group of fluorescent dyes by measuring the increase in their polarization . The ...
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