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
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Page vii
... measured in countless biochemical laboratories. A great variety of sophisticated techniques and an even greater ... measurements for them. In either case, the acceptance of the resulting data and their interpretation can be uncritical or ...
... measured in countless biochemical laboratories. A great variety of sophisticated techniques and an even greater ... measurements for them. In either case, the acceptance of the resulting data and their interpretation can be uncritical or ...
Page 1
... Measurement . A. The Size of Protein Molecules B. Techniques for Measurement . C. Instrumental Calibration . . . . . D. Sources of Artifacts in Measurements from Electron Micrographs . . . . . . . . . . . . Examples of the Application ...
... Measurement . A. The Size of Protein Molecules B. Techniques for Measurement . C. Instrumental Calibration . . . . . D. Sources of Artifacts in Measurements from Electron Micrographs . . . . . . . . . . . . Examples of the Application ...
Page 39
... Measurement Quantitative measurements of macromolecules observed in electron micrographs are important not only because of the intrinsic interest in the size of biological macromolecules, but also because it may be possible to correlate ...
... Measurement Quantitative measurements of macromolecules observed in electron micrographs are important not only because of the intrinsic interest in the size of biological macromolecules, but also because it may be possible to correlate ...
Page 41
... MEASUREMENT 1. General Considerations Measurements from electron micrographs must be carried out at magnifications which are sufficiently great to render negligible the uncertainties in reading a ruler or micrometer. At the same time ...
... MEASUREMENT 1. General Considerations Measurements from electron micrographs must be carried out at magnifications which are sufficiently great to render negligible the uncertainties in reading a ruler or micrometer. At the same time ...
Page 42
... measurements from a number of different areas than by measuring a large number of particles from a single area. The total number of particles measured may vary between 200 and 2000, depending upon the nature of the specimen. Apart from ...
... measurements from a number of different areas than by measuring a large number of particles from a single area. The total number of particles measured may vary between 200 and 2000, depending upon the nature of the specimen. Apart from ...
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