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 43
Page 42
... molecular weight. In view of the many uncertainties in the quantitation of electron microscope observations, a ... molecular weights computed for such a preparation would be misleadingly low. On the other hand, when a histogram reveals a ...
... molecular weight. In view of the many uncertainties in the quantitation of electron microscope observations, a ... molecular weights computed for such a preparation would be misleadingly low. On the other hand, when a histogram reveals a ...
Page 48
... molecular weight of 330,000, established from measurements of sedimentation, diffusion, and viscosity by Shulman (1953) and which corresponds to a molecular volume of 3.87 X 10*19 cm3, was correlated with the observed triad structure ...
... molecular weight of 330,000, established from measurements of sedimentation, diffusion, and viscosity by Shulman (1953) and which corresponds to a molecular volume of 3.87 X 10*19 cm3, was correlated with the observed triad structure ...
Page 50
... molecular weight per unit length relative to that of fibrinogen. Two possible mechanisms, neither of which is unequivocally established as correct at present, could account for these data. As shown in Fig. 12b, the intermediate polymers ...
... molecular weight per unit length relative to that of fibrinogen. Two possible mechanisms, neither of which is unequivocally established as correct at present, could account for these data. As shown in Fig. 12b, the intermediate polymers ...
Page 51
... molecules, partially extended molecules, and short threads. The dimensions of particles in each of these categories are'consistent with the known molecular weight. The proportion of globular particles, judged to be the native form of ...
... molecules, partially extended molecules, and short threads. The dimensions of particles in each of these categories are'consistent with the known molecular weight. The proportion of globular particles, judged to be the native form of ...
Page 85
... structure of globular protein crystals because even the heaviest atom would not have sufficient weight to dominate ... molecular conformation, and the position and orientation of the molecule within the unit cell are practically ...
... structure of globular protein crystals because even the heaviest atom would not have sufficient weight to dominate ... molecular conformation, and the position and orientation of the molecule within the unit cell are practically ...
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