Physical Principles and Techniques of Protein Chemistry, Part 1Physical 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 maps from X-ray methods and the diffraction data from fibrous proteins. The subsequent chapters cover discussions on UV spectroscopy of proteins; luminescence properties of proteins and related compounds; and perturbation and flow methods for evaluation of proteins’ dynamic properties and rate constants. Other chapters deal with the evaluation of proteins’ dielectric properties using dielectric relaxation, electric birefringence, and dichroism techniques. The concluding chapters outline the theoretical and experimental advances of the electrophoretic and gel filtration methods for the study of protein structure and molecular weight. This book is of great value to chemists, biologists, and researchers who have great appreciation of protein chemistry. |
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Page 11
High resolution images of a hole in a carbon film. (a) Slight underfocus. There is
a halo of high electron intensity inside the image of the hole. (A more pronounced
underfocus halo appears in part of Fig. 4a.) A regular granularity is evident in ...
High resolution images of a hole in a carbon film. (a) Slight underfocus. There is
a halo of high electron intensity inside the image of the hole. (A more pronounced
underfocus halo appears in part of Fig. 4a.) A regular granularity is evident in ...
Page 12
Films. Ideally, the continuous specimen support film should be of minimal
electron scattering power (i.e., of maximum “electron-transparency”),
mechanically stable, electrically conductive, stable in the electron beam (i.e., it
should neither ...
Films. Ideally, the continuous specimen support film should be of minimal
electron scattering power (i.e., of maximum “electron-transparency”),
mechanically stable, electrically conductive, stable in the electron beam (i.e., it
should neither ...
Page 13
incorporate many small holes. Methods for preparing such films vary, but have
the common feature of exposing a plastic film to moisture during the evaporation
of an organic solvent. Holes then remain where the water droplets were present.
incorporate many small holes. Methods for preparing such films vary, but have
the common feature of exposing a plastic film to moisture during the evaporation
of an organic solvent. Holes then remain where the water droplets were present.
Page 31
Compounds Used to Effect Negative Contrast The substance used to provide
negative contrast must be a material of high mass density (and thus of high
electron-scattering power), of high solubility, and must form a continuous film
rather than ...
Compounds Used to Effect Negative Contrast The substance used to provide
negative contrast must be a material of high mass density (and thus of high
electron-scattering power), of high solubility, and must form a continuous film
rather than ...
Page 32
film; as discussed above, uranyl formats or acetate films are the most satisfactory
from this point of view. When phosphotungstate stains are employed, pH values
somewhat lower than neutrality are best. Another approach to minimizing ...
film; as discussed above, uranyl formats or acetate films are the most satisfactory
from this point of view. When phosphotungstate stains are employed, pH values
somewhat lower than neutrality are best. Another approach to minimizing ...
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Contents
59 | |
Chapter 3 Ultraviolet Absorption | 101 |
Chapter 4 Fluorescence of Proteins | 171 |
Chapter 5 Perturbation and Flow Techniques | 245 |
Chapter 6 Dielectric Properties of Proteins I Dielectric Relaxation | 291 |
Chapter 7 Dielectric Properties of Proteins II Electric Birefringence and Dichroism | 335 |
Chapter 8 Electrophoresis | 369 |
Chapter 9 Analytical Gel Filtration | 451 |
Author Index | 497 |
Subject Index | 509 |
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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 concentration curve defined denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction diffusion dipole moment Edelhoch effects electric birefringence electric field electron microscope electrophoresis elution volume emission energy enzyme equation equilibrium excitation experimental factor field strength film filters first flow fluorescence fraction frequency gel filtration groups intensity interactions ionic strength ions light macromolecules magnification measured method migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole perturbation phase phenolic phenylalanine photomultiplier Phys plot polarization polymer protein quantum yield ratio reaction reflections relaxation residues ribonuclease rotation shown in Fig significant solution solvent specific specimen spectra structure sufficiently technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone