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 85
Page 7
... effects are the principal sources of contrast. For very small objects, phase-contrast effects may be important. 2. Differential Scattering Contrast Electron scattering by the background (i.e., by the “electron-transparent” support film) ...
... effects are the principal sources of contrast. For very small objects, phase-contrast effects may be important. 2. Differential Scattering Contrast Electron scattering by the background (i.e., by the “electron-transparent” support film) ...
Page 9
... effect of introducing optical path length differences between electrons which travel through different zones of the lens. The resulting phase effects are important in producing contrast in images of structures near the limit of ...
... effect of introducing optical path length differences between electrons which travel through different zones of the lens. The resulting phase effects are important in producing contrast in images of structures near the limit of ...
Page 10
... effects is that contrast is minimal at exact focus. The presence of overfocus fringes tends to confuse the image, but at slight underfocus the image is sharp, and contrast is enhanced by the “highlighting” effect. Virtually all electron ...
... effects is that contrast is minimal at exact focus. The presence of overfocus fringes tends to confuse the image, but at slight underfocus the image is sharp, and contrast is enhanced by the “highlighting” effect. Virtually all electron ...
Page 13
... effects of drying should be avoided. Suitable concentrations of protein solutions for microscopy are of the order of 0.1 mg/ml. With larger particles, such as the small viruses, somewhat higher weight concentrations are required in ...
... effects of drying should be avoided. Suitable concentrations of protein solutions for microscopy are of the order of 0.1 mg/ml. With larger particles, such as the small viruses, somewhat higher weight concentrations are required in ...
Page 14
... 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.
... 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.
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