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 154
... absorbance ( that absorbance giving the smallest relative error of measurement ) with a shot - noise limited system is about 1.0 ( Fig . 21 ) . However , samples with absorb- ances of 2 or 3 are measured nearly as accurately . 0.12 ...
... absorbance ( that absorbance giving the smallest relative error of measurement ) with a shot - noise limited system is about 1.0 ( Fig . 21 ) . However , samples with absorb- ances of 2 or 3 are measured nearly as accurately . 0.12 ...
Page 156
... absorbance at 275 mμ of successive pairs of K2CrO , solutions ( ordinate ) , plotted against the true absorbance of the more concentrated solution ( abscissa ) . O , Measurements made with the Cary 14 spectrophotometer ...
... absorbance at 275 mμ of successive pairs of K2CrO , solutions ( ordinate ) , plotted against the true absorbance of the more concentrated solution ( abscissa ) . O , Measurements made with the Cary 14 spectrophotometer ...
Page 158
... absorbance units.12 Many good spectrophotometers will give an accuracy and reproducibility of 0.0002 absorbance units , so that an absorbance difference of 0.02 can be measured with 1 % accuracy . If spectra are recorded slowly , using ...
... absorbance units.12 Many good spectrophotometers will give an accuracy and reproducibility of 0.0002 absorbance units , so that an absorbance difference of 0.02 can be measured with 1 % accuracy . If spectra are recorded slowly , using ...
Contents
Electron Microscopy of Globular Proteins | 2 |
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Copyright | |
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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