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 x
... Temperature-Jump Techniques . References . . . . . . . . 6. Dielectric Properties of Proteins I. Dielectric Relaxation. Shim. Takashima. Glossary of Symbols . I. Introduction . . II. Dielectrics in a Static Field 245 247 247 278 288 289 ...
... Temperature-Jump Techniques . References . . . . . . . . 6. Dielectric Properties of Proteins I. Dielectric Relaxation. Shim. Takashima. Glossary of Symbols . I. Introduction . . II. Dielectrics in a Static Field 245 247 247 278 288 289 ...
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... . The effects of room temperature air-drying Of macromolecules are difficult to assess. “Drop patterns” are remarkably variable; in general, material tends to concentrate at drop edges and centers. These 14 ELIZABETH M. SLAYTER.
... . The effects of room temperature air-drying Of macromolecules are difficult to assess. “Drop patterns” are remarkably variable; in general, material tends to concentrate at drop edges and centers. These 14 ELIZABETH M. SLAYTER.
Page 17
... temperature. Contamination then deposits on the cold surface, rather than on the specimen. With the use of such devices, which are commercially available, contamination can be reduced to negligible levels during at least a 15-minute ...
... temperature. Contamination then deposits on the cold surface, rather than on the specimen. With the use of such devices, which are commercially available, contamination can be reduced to negligible levels during at least a 15-minute ...
Page 37
... temperature of liquid nitrogen (—196°C). Moisture is then slowly removed by sublimation in a vacuum. While surface tension effects are not entirely avoided, the sublimation process is a much more gentle one than normal drying. Particles ...
... temperature of liquid nitrogen (—196°C). Moisture is then slowly removed by sublimation in a vacuum. While surface tension effects are not entirely avoided, the sublimation process is a much more gentle one than normal drying. Particles ...
Page 38
... temperature” which is characteristic Of each substance. Thus, when the temperature of a liquid is raised beyond its critical point, the material is converted “imperceptibly” to a gas; for C02, this occurs at 31°C. The wet electron ...
... temperature” which is characteristic Of each substance. Thus, when the temperature of a liquid is raised beyond its critical point, the material is converted “imperceptibly” to a gas; for C02, this occurs at 31°C. The wet electron ...
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