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 1-5 of 93
Page ii
... Molecular Photobiology: Inactivation and Recovery. 1969 RONALD BENTLEY. Molecular Asymmetry in Biology. Volume I—1969. Volume II—1970 JACINTO STEINHARDT AND JACQUELINE A. REYNOLDS. Multiple Equilibria in Protein. 1969 DOUGLAS POLAND AND ...
... Molecular Photobiology: Inactivation and Recovery. 1969 RONALD BENTLEY. Molecular Asymmetry in Biology. Volume I—1969. Volume II—1970 JACINTO STEINHARDT AND JACQUELINE A. REYNOLDS. Multiple Equilibria in Protein. 1969 DOUGLAS POLAND AND ...
Page 2
... molecules. In fact, the resolution achieved in the observation of biological specimens is considerably poorer, being at best only about 10 A. The limitations which preclude full exploitation of instrumental resolving power are lack of ...
... molecules. In fact, the resolution achieved in the observation of biological specimens is considerably poorer, being at best only about 10 A. The limitations which preclude full exploitation of instrumental resolving power are lack of ...
Page 12
... molecules and other biological materials is little different from that of the carbon support. Films of adequate ... molecular structure. Such patterns must be observed in a substantial number of particles before they can be considered ...
... molecules and other biological materials is little different from that of the carbon support. Films of adequate ... molecular structure. Such patterns must be observed in a substantial number of particles before they can be considered ...
Page 26
... molecules as small as 10 to 20A in diameter can be detected, especially at relatively large shadow ratios. The ultimate limitation of the technique is the substructure of the evaporated metal itself. Individual metal atoms are not ...
... molecules as small as 10 to 20A in diameter can be detected, especially at relatively large shadow ratios. The ultimate limitation of the technique is the substructure of the evaporated metal itself. Individual metal atoms are not ...
Page 32
... molecule to significantly improve its contrast. Somewhat larger particles, such as ribosomes, have been more suitable specimens for positive staining techniques ... molecules of the enzyme RNA-polymerase attached to 32 ELIZABETH M. SLAYTER.
... molecule to significantly improve its contrast. Somewhat larger particles, such as ribosomes, have been more suitable specimens for positive staining techniques ... molecules of the enzyme RNA-polymerase attached to 32 ELIZABETH M. SLAYTER.
Contents
Chapter 2 XRay Methods | 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