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 40
Page 36
... residues form upon exposure to air, and contribute to the background noise of micrographs. During the process of drying down, the ionic concentration and, in many cases, the pH of solutions change rapidly. The importance of these ...
... residues form upon exposure to air, and contribute to the background noise of micrographs. During the process of drying down, the ionic concentration and, in many cases, the pH of solutions change rapidly. The importance of these ...
Page 65
... residues related by symmetry. Part of the shaded residue lies outside the cell but an equivalent set of atoms appears within the cell 6.88A further along the chain. The shaded alanyl residue, --NH ——CH(CH:)—-CO—, may be taken as the ...
... residues related by symmetry. Part of the shaded residue lies outside the cell but an equivalent set of atoms appears within the cell 6.88A further along the chain. The shaded alanyl residue, --NH ——CH(CH:)—-CO—, may be taken as the ...
Page 66
... residues, this operation would involve a change to the D-configuration and centers of symmetry are therefore not found in protein crystals. However, it is possible for a projection Of a protein crystal to possess a center of symmetry ...
... residues, this operation would involve a change to the D-configuration and centers of symmetry are therefore not found in protein crystals. However, it is possible for a projection Of a protein crystal to possess a center of symmetry ...
Page 68
... residue and by the repeated opera— tion of the symmetry elements (rotation and screw axes) the remainder of the atoms in the unit cell can be generated. IV. The Reciprocal Luflice When a crystal is successively moved through a series of ...
... residue and by the repeated opera— tion of the symmetry elements (rotation and screw axes) the remainder of the atoms in the unit cell can be generated. IV. The Reciprocal Luflice When a crystal is successively moved through a series of ...
Page 96
... residues. Z 6 " m n l | 0 I0 0 9 /7 | -| 7 o 2 s c p | -2 4 o l a | —a l o 0 o - -| a -| r 0 2 z. e 21rqu FIG. 22. Idealized diffraction pattern (right) given by a discontinuous helix (left) with 10 units in three turns. P is the pitch ...
... residues. Z 6 " m n l | 0 I0 0 9 /7 | -| 7 o 2 s c p | -2 4 o l a | —a l o 0 o - -| a -| r 0 2 z. e 21rqu FIG. 22. Idealized diffraction pattern (right) given by a discontinuous helix (left) with 10 units in three turns. P is the pitch ...
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