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 ... |
From inside the book
Results 1-3 of 92
Page 119
... difference spectrum will have the wave- length dependence of the difference absorption coefficient ( Fig . 4 ) . Sim- ilarly , at any fixed wavelength and chromophore concentration , the optical density difference measured as a function ...
... difference spectrum will have the wave- length dependence of the difference absorption coefficient ( Fig . 4 ) . Sim- ilarly , at any fixed wavelength and chromophore concentration , the optical density difference measured as a function ...
Page 141
... difference spectrum , Fig . 16 , is almost identical with the solvent perturbation difference spectrum of tryptophan produced by ethylene glycol ( Fig . 9 ) . The magnitude ( height ) of the difference spec- trum has the same pH ...
... difference spectrum , Fig . 16 , is almost identical with the solvent perturbation difference spectrum of tryptophan produced by ethylene glycol ( Fig . 9 ) . The magnitude ( height ) of the difference spec- trum has the same pH ...
Page 158
... difference of 0.02 can be measured with 1 % accuracy . If spectra are recorded slowly , using a long time constant in order to im- prove signal - to - noise ratio , it should be established that the zero drift of the instrument is not ...
... difference of 0.02 can be measured with 1 % accuracy . If spectra are recorded slowly , using a long time constant in order to im- prove signal - to - noise ratio , it should be established that the zero drift of the instrument is not ...
Contents
Electron Microscopy of Globular Proteins | 2 |
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Copyright | |
50 other sections not shown
Other editions - View all
Common terms and phrases
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