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 88
Page 40
... group of small spheres of different sizes tend to seem uniform to the inexperienced observer. Thus, conclusions from electron microscope observations that a suspension of particles is “homogeneous” are meaningful only if supported by ...
... group of small spheres of different sizes tend to seem uniform to the inexperienced observer. Thus, conclusions from electron microscope observations that a suspension of particles is “homogeneous” are meaningful only if supported by ...
Page 44
... groups of particles are in contact before shadowing, since the individual members of the group may then seem obviously smaller than isolated particles. The particle diameter, measured through its center, is thus increased by a distance ...
... groups of particles are in contact before shadowing, since the individual members of the group may then seem obviously smaller than isolated particles. The particle diameter, measured through its center, is thus increased by a distance ...
Page 59
... Group . D. The Asymmetric Unit . IV. The Reciprocal Lattice V. The Structure Factor VI. Fourier Synthesis . . . A. Sections and Projections B. Resolving Power . . . . C. Thermal Vibrations and Disorder D. Series Termination Errors VII ...
... Group . D. The Asymmetric Unit . IV. The Reciprocal Lattice V. The Structure Factor VI. Fourier Synthesis . . . A. Sections and Projections B. Resolving Power . . . . C. Thermal Vibrations and Disorder D. Series Termination Errors VII ...
Page 66
... group of atoms is repeated at intervals of 360/'N degrees rotation about the axis. In the case illustrated in (b), N I 2 and the rotation is 180°. An N—fold screw axis parallel to c, for example, involves a simultaneous rotation of 360 ...
... group of atoms is repeated at intervals of 360/'N degrees rotation about the axis. In the case illustrated in (b), N I 2 and the rotation is 180°. An N—fold screw axis parallel to c, for example, involves a simultaneous rotation of 360 ...
Page 67
... GROUP Once the shape of the unit cell is known, a second important property of the crystal termed the space group can ... groups are to be found in the International Tables for X-Ray Crystallography I (see Lonsdale, 1952). Occasionally ...
... GROUP Once the shape of the unit cell is known, a second important property of the crystal termed the space group can ... groups are to be found in the International Tables for X-Ray Crystallography I (see Lonsdale, 1952). Occasionally ...
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