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 66
... parameter must be specified and is written as a suffix in the symbol for the symmetry axis. If, for example, there were a 43 screw axis parallel to 0, similar points in the crystal would be related by a simultaneous rotation Of 90 ...
... parameter must be specified and is written as a suffix in the symbol for the symmetry axis. If, for example, there were a 43 screw axis parallel to 0, similar points in the crystal would be related by a simultaneous rotation Of 90 ...
Page 75
... parameter B in Eq. (9) is a measure of the rootmean-square displacement of an atom from its average position (12,17,112) in the cell and is related to it as follows. B. = 812(u. _. W. = 812(1). -. 1'»)? = we». -. m2. (10). The combined ...
... parameter B in Eq. (9) is a measure of the rootmean-square displacement of an atom from its average position (12,17,112) in the cell and is related to it as follows. B. = 812(u. _. W. = 812(1). -. 1'»)? = we». -. m2. (10). The combined ...
Page 81
... parameters are adjusted simultaneously to reduce the discrepancy between the observed and calculated structure amplitudes to a minimum. As each atom requires three parameters to define its position and three to describe its thermal ...
... parameters are adjusted simultaneously to reduce the discrepancy between the observed and calculated structure amplitudes to a minimum. As each atom requires three parameters to define its position and three to describe its thermal ...
Page 83
... parameters may be obtained subsequently by a least-squares refinement. The heavy atom method has been used successfully with molecules containing up to about a hundred atoms, excluding hydrogen (Hodgkin, 1965) and as demonstrated in Fig ...
... parameters may be obtained subsequently by a least-squares refinement. The heavy atom method has been used successfully with molecules containing up to about a hundred atoms, excluding hydrogen (Hodgkin, 1965) and as demonstrated in Fig ...
Page 86
... parameters deduced from the difference Patterson must be refined (Phillips, 1966). An important aspect of this refinement is that lack of isomorphism, incomplete occupancy of the heavy atom site, and additional binding sites can be ...
... parameters deduced from the difference Patterson must be refined (Phillips, 1966). An important aspect of this refinement is that lack of isomorphism, incomplete occupancy of the heavy atom site, and additional binding sites can be ...
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