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 85
Page 18
... determining that pair Of values of magnitude and direction which exactly balance the asymmetry of the main lens, thus rendering the net ... determined, it is main— FIG. 4. Astigmatic images of a hole in a carbon 18 ELIZABETH M. SLAYTER.
... determining that pair Of values of magnitude and direction which exactly balance the asymmetry of the main lens, thus rendering the net ... determined, it is main— FIG. 4. Astigmatic images of a hole in a carbon 18 ELIZABETH M. SLAYTER.
Page 24
... determined by the distance of the specimen from the evaporation source (usually about 5—10 cm), the density of the metal, and the shadowing angle. For platinum shadowing, a calculated thickness of 20 A is approximately correct, i.e. ...
... determined by the distance of the specimen from the evaporation source (usually about 5—10 cm), the density of the metal, and the shadowing angle. For platinum shadowing, a calculated thickness of 20 A is approximately correct, i.e. ...
Page 25
... determined for each micrograph by measuring the lengths of shadows cast by polystyrene spheres within the recorded area. Polystyrene spheres are usually included in preparations of macromolecules; as already mentioned, they are sprayed ...
... determined for each micrograph by measuring the lengths of shadows cast by polystyrene spheres within the recorded area. Polystyrene spheres are usually included in preparations of macromolecules; as already mentioned, they are sprayed ...
Page 42
... determined exactly by a careful comparison of print and plate. Pairs of prominent objects are located on both print ... determination of molecular weight. In view of the many uncertainties in the quantitation of electron microscope ...
... determined exactly by a careful comparison of print and plate. Pairs of prominent objects are located on both print ... determination of molecular weight. In view of the many uncertainties in the quantitation of electron microscope ...
Page 43
... determined by observation of shadowed particles which are known to remain spherical during preparation for electron microscopy. For this purpose, polystyrene latex spheres are included in shadow-cast preparations. Thus, for example, in ...
... determined by observation of shadowed particles which are known to remain spherical during preparation for electron microscopy. For this purpose, polystyrene latex spheres are included in shadow-cast preparations. Thus, for example, in ...
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