Physical Principles and Techniques of Protein Chemistry Part A, Part 1Sydney 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 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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Results 1-5 of 63
Page 6
... defined as in Eq. (1) Percent contrast = M X 100 (1) Ibaokgrou n cl where 1pm.“. is the intensity of the image point and Ibackgmund is that of its surroundings. Resolution refers to the smallest separation of points which can in fact be ...
... defined as in Eq. (1) Percent contrast = M X 100 (1) Ibaokgrou n cl where 1pm.“. is the intensity of the image point and Ibackgmund is that of its surroundings. Resolution refers to the smallest separation of points which can in fact be ...
Page 11
... defined at this setting. The structure of the carbon film has disappeared. (c) Slight overfocus. of the particles of interest. (On the other hand, for. There is a fringe of high electron intensity outside the image of the hole, and ...
... defined at this setting. The structure of the carbon film has disappeared. (c) Slight overfocus. of the particles of interest. (On the other hand, for. There is a fringe of high electron intensity outside the image of the hole, and ...
Page 20
... defined. In-focus images are of noticeably lower contrast, although edges, upon close examination, are found to be defined most clearly, while overfocus images are again of higher contrast but conspicuously blurred. The detection of ...
... defined. In-focus images are of noticeably lower contrast, although edges, upon close examination, are found to be defined most clearly, while overfocus images are again of higher contrast but conspicuously blurred. The detection of ...
Page 23
... defined. (0) Same micrograph as (b) at higher magnification. Significant features of specimen structure have become relatively less Obvious because of the excessive magnification of background grain. The shadow-casting technique has ...
... defined. (0) Same micrograph as (b) at higher magnification. Significant features of specimen structure have become relatively less Obvious because of the excessive magnification of background grain. The shadow-casting technique has ...
Page 36
... defined images of these particles in shadow-cast preparations, whereas if rewetting and redrying of such suspensions occurs, only heterogeneous debris results. Since no means exists for the direct visualization of the particles in their ...
... defined images of these particles in shadow-cast preparations, whereas if rewetting and redrying of such suspensions occurs, only heterogeneous debris results. Since no means exists for the direct visualization of the particles in their ...
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 |
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