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 31
Page 4
... film. Those portions of the film and specimen may be viewed which do not overlie the support wires. Means are provided for external manipulation of the specimen within the evacuated column. Electron images are detected on a fluorescent ...
... film. Those portions of the film and specimen may be viewed which do not overlie the support wires. Means are provided for external manipulation of the specimen within the evacuated column. Electron images are detected on a fluorescent ...
Page 7
... film) occurs principally within small angles, while scattering by “electron-opaque” specimen points is spread over larger angles. As shown in Fig. 2a, electrons scattered Within some angle a are included Within the aperture of the ...
... film) occurs principally within small angles, while scattering by “electron-opaque” specimen points is spread over larger angles. As shown in Fig. 2a, electrons scattered Within some angle a are included Within the aperture of the ...
Page 8
... film which is itself usually composed of carbon, so that the electron scattering power of the support necessarily approaches that of the specimen. The difficulties so introduced may be compared to those of using a deeply colored stained ...
... film which is itself usually composed of carbon, so that the electron scattering power of the support necessarily approaches that of the specimen. The difficulties so introduced may be compared to those of using a deeply colored stained ...
Page 10
... film at three focal levels. Higher electron intensity is found outside the edge of the hole at underfocus settings of the microscope. Fringe and geometrical edge coincide at exact focus, while at overfocus the fringe of high intensity ...
... film at three focal levels. Higher electron intensity is found outside the edge of the hole at underfocus settings of the microscope. Fringe and geometrical edge coincide at exact focus, while at overfocus the fringe of high intensity ...
Page 11
... film is most clearly defined at this setting. The structure of the carbon film has disappeared. (c) Slight overfocus. of the particles of interest. (On the other hand, for. There is a fringe of high electron intensity outside the image ...
... film is most clearly defined at this setting. The structure of the carbon film has disappeared. (c) Slight overfocus. of the particles of interest. (On the other hand, for. There is a fringe of high electron intensity outside the image ...
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