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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Page ix
... . . . . Methods of Structure Determination . Fiber Diffraction Further Reading References vii xiii 21 39 48 55 “6565050501 gasagp-oooot—oso 3. Ultraviolet Absorption John W. Donovan Glossary of Symbols . Table of Contents.
... . . . . Methods of Structure Determination . Fiber Diffraction Further Reading References vii xiii 21 39 48 55 “6565050501 gasagp-oooot—oso 3. Ultraviolet Absorption John W. Donovan Glossary of Symbols . Table of Contents.
Page 4
... and may thus be limited by restricting the aperture. Ultimately, however, spreading of point images due to diffraction sets a lower limit I'l Lamp Electron gun Condenser IE ICondenser lens lens Specimen 4 ELIZABETH M. SLAYTER.
... and may thus be limited by restricting the aperture. Ultimately, however, spreading of point images due to diffraction sets a lower limit I'l Lamp Electron gun Condenser IE ICondenser lens lens Specimen 4 ELIZABETH M. SLAYTER.
Page 9
... diffraction just balance. When the size of the aperture is reduced, electrons which pass through the lens margins are excluded from the image altogether, as shown in Fig. 2b. Thus the background intensity of aberrant electrons is ...
... diffraction just balance. When the size of the aperture is reduced, electrons which pass through the lens margins are excluded from the image altogether, as shown in Fig. 2b. Thus the background intensity of aberrant electrons is ...
Page 10
... diffraction theory gives the approximate loss of resolving power Ar which corresponds to defocusing of the lens by a change in focal length of Af Ar = VAAf (2) where A is the electron wavelength. Qualitatively, it may be said that fine ...
... diffraction theory gives the approximate loss of resolving power Ar which corresponds to defocusing of the lens by a change in focal length of Af Ar = VAAf (2) where A is the electron wavelength. Qualitatively, it may be said that fine ...
Page 27
... diffraction measurements. While the periodicity seen in the TMV rods by Hart is generally very similar to that of the background, its direction varies with the orientation of the virus particle. In summary, the use of ultrahigh vacuum ...
... diffraction measurements. While the periodicity seen in the TMV rods by Hart is generally very similar to that of the background, its direction varies with the orientation of the virus particle. In summary, the use of ultrahigh vacuum ...
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