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 48
Page 50
... peak lengths obtained as a function Of pH is shown in Fig. 12d. Minimum lengths, which approximate to the 240A spacing found in fibrin, occur near the isoelectric point at pH 5.5. Since, however, extensive shrinkage of molecules might ...
... peak lengths obtained as a function Of pH is shown in Fig. 12d. Minimum lengths, which approximate to the 240A spacing found in fibrin, occur near the isoelectric point at pH 5.5. Since, however, extensive shrinkage of molecules might ...
Page 53
... peaks are observed during ultracentrifugation of the digest. Electron microscopy of this type of preparation shows that the peaks correspond to complete- and split-“heads,” respectively. Further digestion eliminates the more rapidly ...
... peaks are observed during ultracentrifugation of the digest. Electron microscopy of this type of preparation shows that the peaks correspond to complete- and split-“heads,” respectively. Further digestion eliminates the more rapidly ...
Page 78
... peaks associated with lighter atoms (e.g., Jeffrey, 1951). The effect may be eliminated by applying an artificial temperature factor to the data. The observed structure amplitudes are multiplied by a term exp(——Bd*'/4), where B has been ...
... peaks associated with lighter atoms (e.g., Jeffrey, 1951). The effect may be eliminated by applying an artificial temperature factor to the data. The observed structure amplitudes are multiplied by a term exp(——Bd*'/4), where B has been ...
Page 82
... Peaks in the Patterson function occur at positions corresponding to interatomic vectors in the original structure ... peak A; similarly, vectors B1 and B2 are among those which contribute to peak B. If potassium atoms were situated in ...
... Peaks in the Patterson function occur at positions corresponding to interatomic vectors in the original structure ... peak A; similarly, vectors B1 and B2 are among those which contribute to peak B. If potassium atoms were situated in ...
Page 83
... peaks appear close to the true positions of the lighter atoms. The peaks associated with the hydrogen atoms are very weak and are lost in the spurious background. The accuracy of the map can be improved by Fourier refinement. Instead of ...
... peaks appear close to the true positions of the lighter atoms. The peaks associated with the hydrogen atoms are very weak and are lost in the spurious background. The accuracy of the map can be improved by Fourier refinement. Instead of ...
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