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. |
From inside the book
Results 6-10 of 97
Page 2
... structure. It is even difi'icult to determine the extent to which the ultrastructure has been preserved, since the ... structures. Measurement from electron micrographs is discussed, and some illustrative examples Of the study of protein ...
... structure. It is even difi'icult to determine the extent to which the ultrastructure has been preserved, since the ... structures. Measurement from electron micrographs is discussed, and some illustrative examples Of the study of protein ...
Page 9
... structures near the limit of resolution. Such images must be interpreted with caution, since variations in intensity may not be directly related to the structure of the specimen. The out-of-focus effects discussed below are also a phase ...
... structures near the limit of resolution. Such images must be interpreted with caution, since variations in intensity may not be directly related to the structure of the specimen. The out-of-focus effects discussed below are also a phase ...
Page 11
... 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 graininess has reappeared in 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 graininess has reappeared in the ...
Page 12
... Structure within the film may thus easily be confused with fine structure in the supported particles. High-resolution microscopy reveals structure in carbon films down to the finest level observable, which is about 5 A. The observation ...
... Structure within the film may thus easily be confused with fine structure in the supported particles. High-resolution microscopy reveals structure in carbon films down to the finest level observable, which is about 5 A. The observation ...
Page 13
... structure. Intensities originating from the film could then be subtracted systematically from those produced by the image. The possibility remains a hypothetical one at present, since crystalline films of a usefully small thickness and ...
... structure. Intensities originating from the film could then be subtracted systematically from those produced by the image. The possibility remains a hypothetical one at present, since crystalline films of a usefully small thickness and ...
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