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 83
Page 1
... Determination of Sedimentation Coefficients C. Detection of Heterogeneity . 37 37 37 38 42 D. Interpretation of Sedimentation Coefficient Measurements V. Sedimentation Equilibrium of Noninteracting Solutes 43 45 A. Available Methods ...
... Determination of Sedimentation Coefficients C. Detection of Heterogeneity . 37 37 37 38 42 D. Interpretation of Sedimentation Coefficient Measurements V. Sedimentation Equilibrium of Noninteracting Solutes 43 45 A. Available Methods ...
Page 4
... determination of protein concentration inaccurate . Sedimentation equilibrium experiments may be too time consuming for some purposes , in which case the Archibald method , which exploits the equilibrium that always exists at the ...
... determination of protein concentration inaccurate . Sedimentation equilibrium experiments may be too time consuming for some purposes , in which case the Archibald method , which exploits the equilibrium that always exists at the ...
Page 5
... determined by the rotor speed , the density difference between the solute and the solution , and most importantly , the molecular weight and shape of the protein molecule concerned . Thus for a given solution and centrifugal field ...
... determined by the rotor speed , the density difference between the solute and the solution , and most importantly , the molecular weight and shape of the protein molecule concerned . Thus for a given solution and centrifugal field ...
Page 15
... determination of the density increment . For example , if c , is expressed in terms of a weight of dry isoionic ... determined at a particular x distance in the ultracentrifuge cell , and measurements are carried out at such a low ...
... determination of the density increment . For example , if c , is expressed in terms of a weight of dry isoionic ... determined at a particular x distance in the ultracentrifuge cell , and measurements are carried out at such a low ...
Page 17
... determined if the virial coefficient is known or if ideality may be assumed . As explained in Section II , B , 2 ... determine the protein concentration in the cell , error will occur if , due to interaction , the low molecular weight ...
... determined if the virial coefficient is known or if ideality may be assumed . As explained in Section II , B , 2 ... determine the protein concentration in the cell , error will occur if , due to interaction , the low molecular weight ...
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