Physical Principles and Techniques of Protein Chemistry Part B, Part 2Sydney Leach Physical Principles and Techniques of Protein Chemistry, Part B deals with the theories and application of selected physical methods in protein chemistry evaluation. This book is divided into seven chapters that cover the ultracentrifugal analysis, light scattering, infrared (IR) methods, nuclear magnetic resonance (NMR) spectroscopy, and differential thermal analysis of protein properties. This text first describes the fundamental ideas and methodology of sedimentation analysis of ideal noninteracting solutes and the problems of nonideality and solute-solute interaction. This book then deals with the problems involved in the interpretation of viscometric data for evaluation of intrinsic viscosity of proteins. The following chapters examine the principles, measurement and analysis of spectra, and experimental techniques of light scattering, IR, and NMR spectroscopic methods. Discussions on coordination phenomena, identification of binding sites, and ion binding in the crystalline state and in protein solutions are included. The concluding chapter presents some examples of protein analysis using differential thermal analysis technique. 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 21
Page xiii
... Flow Techniques B. H. Havsteen Dielectric Properties of Proteins I. Dielectric Relaxation Shiro Takashima Dielectric Properties of Proteins II . Electric Birefringence and Dichroism Koshiro Yoshioka and Hiroshi Watanabe Electrophoresis ...
... Flow Techniques B. H. Havsteen Dielectric Properties of Proteins I. Dielectric Relaxation Shiro Takashima Dielectric Properties of Proteins II . Electric Birefringence and Dichroism Koshiro Yoshioka and Hiroshi Watanabe Electrophoresis ...
Page 11
... flow of one component may markedly influence the flow of the others . Thus , interpretation of changes in the apparent sedimentation coefficient of the protein component due to the addition of another component must be made with caution ...
... flow of one component may markedly influence the flow of the others . Thus , interpretation of changes in the apparent sedimentation coefficient of the protein component due to the addition of another component must be made with caution ...
Page 19
... flow onto the top of a solution while the cell is rotating in the ultracentrifuge at low speed ( below 10,000 rpm ) . In this manner an artificial boundary is formed between solution and solvent . Such boundaries are used for the direct ...
... flow onto the top of a solution while the cell is rotating in the ultracentrifuge at low speed ( below 10,000 rpm ) . In this manner an artificial boundary is formed between solution and solvent . Such boundaries are used for the direct ...
Page 55
... flow of the solute at any point in the cell when equilibrium is established . Archibald ( 1947 ) pointed out that during the approach to sedimentation equilibrium the condition of no net flow applies continually at the upper and lower ...
... flow of the solute at any point in the cell when equilibrium is established . Archibald ( 1947 ) pointed out that during the approach to sedimentation equilibrium the condition of no net flow applies continually at the upper and lower ...
Page 60
... flow of one solute and another and physical interactions can influence the con- centration distribution of a solute at sedimentation equilibrium . B. SOLUTES THAT INTERACT AT A RATE THAT IS SLOW COMPARED TO THE RATE OF SEDIMENTATION If ...
... flow of one solute and another and physical interactions can influence the con- centration distribution of a solute at sedimentation equilibrium . B. SOLUTES THAT INTERACT AT A RATE THAT IS SLOW COMPARED TO THE RATE OF SEDIMENTATION If ...
Contents
1 | |
Chapter 11 Viscosity | 99 |
Chapter 12 Light Scattering | 147 |
Chapter 13 Infrared Methods | 213 |
Chapter 14 Nuclear Magnetic Resonance Spectroscopy | 275 |
Chapter 15 Binding of Protons and Other Ions | 365 |
Chapter 16 Differential Thermal Analysis | 437 |
Author Index | 463 |
Subject Index | 479 |
Common terms and phrases
absorption anions atoms band beam binding Biochemistry Biol bond bound Bradbury calculated cell chain changes Chem chemical shifts cm-¹ coil complex component concentration conformational constant copper(II crystalline denaturation density gradient dependence determined differential thermal analysis effect electron enzyme equation equilibrium field Fraser frequency fringe Gurd histidine hydrogen ion imidazole imidazole groups instrument interaction intrinsic viscosity Jardetzky ligand light scattering light-scattering line width lysozyme macromolecule magnetic measured meniscus metal ion method molecular weight molecule myoglobin Natl nuclei observed obtained optical density orientation parameters partial specific volume particle peak peptide Phys Polymer Polymer Sci Proc protein solution protons random coil reaction reference refractive index region relaxation residues resonance RNase rotation rotor sample schlieren Section sedimentation coefficient slit solvent spectra spectrum speed structure studies Tanford technique temperature thermogram Timasheff tion titration transition transmittance ultracentrifuge values velocity Vinograd viscometer zero