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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Results 6-10 of 84
Page 39
... solutions studied in the electron microscope must be so great as to leave no doubt that the particles observed in micrographs are in fact the same as those studied in solution. This apparently simple criterion is Often quite difficult ...
... solutions studied in the electron microscope must be so great as to leave no doubt that the particles observed in micrographs are in fact the same as those studied in solution. This apparently simple criterion is Often quite difficult ...
Page 42
... solution is being studied. Any one electron microscope field is thus too small a proportion of the original solution to be considered as representative of the whole. Many areas of the specimen should be scanned before any decision is ...
... solution is being studied. Any one electron microscope field is thus too small a proportion of the original solution to be considered as representative of the whole. Many areas of the specimen should be scanned before any decision is ...
Page 48
... solutions of fibrinogen at pH 9.5 in close correlation with hydrodynamic data (Hall and Slayter, 1959). Although a ... solution. It was considered that many Of the shorter lengths resulted from shrinkage during drying. The molecular ...
... solutions of fibrinogen at pH 9.5 in close correlation with hydrodynamic data (Hall and Slayter, 1959). Although a ... solution. It was considered that many Of the shorter lengths resulted from shrinkage during drying. The molecular ...
Page 50
... solution. Unfortunately, studies of this point have not yielded conclusive data. Recently, it has been found that tactoids of fibrinogen molecules may be formed (i.e., without activation by thrombin) when the salt concentration of the ...
... solution. Unfortunately, studies of this point have not yielded conclusive data. Recently, it has been found that tactoids of fibrinogen molecules may be formed (i.e., without activation by thrombin) when the salt concentration of the ...
Page 51
... solutions of bovine serum albumin falls below 4.0. Electron microscopy of this system yields observations Which can be correlated with the data obtained in solution, but which at the same time reveal the limitations of techniques ...
... solutions of bovine serum albumin falls below 4.0. Electron microscopy of this system yields observations Which can be correlated with the data obtained in solution, but which at the same time reveal the limitations of techniques ...
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