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 6-10 of 90
Page 43
... measured length of the shadow cast by particle pamde helght = effective shadow ratio X total magnification (11) Measurements of the lengths of shadows is a somewhat subjective procedure since, even under ideal conditions, the tips of ...
... measured length of the shadow cast by particle pamde helght = effective shadow ratio X total magnification (11) Measurements of the lengths of shadows is a somewhat subjective procedure since, even under ideal conditions, the tips of ...
Page 44
... measured through its center, is thus increased by a distance which is determined by the amount of metal deposited. FIG. 9. FIG. 10. FIG. 9 (left). Measurement of shadow lengths of shadow-cast particles. The length is measured from the ...
... measured through its center, is thus increased by a distance which is determined by the amount of metal deposited. FIG. 9. FIG. 10. FIG. 9 (left). Measurement of shadow lengths of shadow-cast particles. The length is measured from the ...
Page 45
... measurements of molecular dimensions by electron microscopy. Unlike the light microscope, the electron microscope makes ... measured. A permanent record of calibration data should be kept. For a more immediate check on magnification, the ...
... measurements of molecular dimensions by electron microscopy. Unlike the light microscope, the electron microscope makes ... measured. A permanent record of calibration data should be kept. For a more immediate check on magnification, the ...
Page 46
... measured. The specimen should not be easily damaged or distorted, and the spacings should be easy to Observe. In practice, the most useful calibration specimens are replicas of diffraction gratings. These specimens are now obtainable ...
... measured. The specimen should not be easily damaged or distorted, and the spacings should be easy to Observe. In practice, the most useful calibration specimens are replicas of diffraction gratings. These specimens are now obtainable ...
Page 47
... measurements from shadow-cast preparations are also somewhat uncertain on account of difficulties in locating the tips of shadows cast by the particles. Diameters measured from negatively contrasted particles seem to be equally suspect ...
... measurements from shadow-cast preparations are also somewhat uncertain on account of difficulties in locating the tips of shadows cast by the particles. Diameters measured from negatively contrasted particles seem to be equally suspect ...
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