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. |
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Page xi
... Equation of Forced Diffusion in the Case of Electrophoresis . . . . . . . . . 335 336 339 350 358 365 366 369 371 373 379 420 441 V. Interpretation of Elution Profiles in Terms of Solute Composition. Appendix B. Formulation of a Theory ...
... Equation of Forced Diffusion in the Case of Electrophoresis . . . . . . . . . 335 336 339 350 358 365 366 369 371 373 379 420 441 V. Interpretation of Elution Profiles in Terms of Solute Composition. Appendix B. Formulation of a Theory ...
Page 73
... Equation (6) may be simplified by writing F (hkl) as |F(hlcl)] exp [ia(hlcl)] and discarding the imaginary part of the summation, since p(xyz) is always real, giving p(xyz) = TI, 2 2 2 lF(hkl)| cos [21r(h:r + Icy + lz) — a(hkl)] (7) h ...
... Equation (6) may be simplified by writing F (hkl) as |F(hlcl)] exp [ia(hlcl)] and discarding the imaginary part of the summation, since p(xyz) is always real, giving p(xyz) = TI, 2 2 2 lF(hkl)| cos [21r(h:r + Icy + lz) — a(hkl)] (7) h ...
Page 75
... Equation (9) implies that the variations in the coordinates are equally likely to occur in any direction. The exponential term causes the atomic scattering to decrease with increasing d* (Fig. 10) and with some protein crystals the ...
... Equation (9) implies that the variations in the coordinates are equally likely to occur in any direction. The exponential term causes the atomic scattering to decrease with increasing d* (Fig. 10) and with some protein crystals the ...
Page 124
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Page 145
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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