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 41
Page ix
... Menisci Only 55 VII . Sedimentation Behavior of Interacting Solutes VIII . Zonal Analytical Velocity Sedimentation . IX . Isopycnic Density Gradient Sedimentation X. A Brief Comparison of Some Commercially Available Ultracentrifuges ...
... Menisci Only 55 VII . Sedimentation Behavior of Interacting Solutes VIII . Zonal Analytical Velocity Sedimentation . IX . Isopycnic Density Gradient Sedimentation X. A Brief Comparison of Some Commercially Available Ultracentrifuges ...
Page 1
... Menisci Only B. Advantages and Limitations of the Method C. Experimental Conditions Necessary for a Reliable Result D. Methods of Calculation VII . Sedimentation Behavior of Interacting Solutes A. Introduction 55 55 55 56 56 57 59 59 1 ...
... Menisci Only B. Advantages and Limitations of the Method C. Experimental Conditions Necessary for a Reliable Result D. Methods of Calculation VII . Sedimentation Behavior of Interacting Solutes A. Introduction 55 55 55 56 56 57 59 59 1 ...
Page 4
... meniscus , may be employed . With impure preparations or if the amount of protein available is very small , it may be prudent to use zonal analytical techniques in which very small quantities of protein are sedimented as zones ...
... meniscus , may be employed . With impure preparations or if the amount of protein available is very small , it may be prudent to use zonal analytical techniques in which very small quantities of protein are sedimented as zones ...
Page 5
... meniscus between the solution and a heavy liquid that is added to the cell to give it a trans- parent bottom . In a typical sedimentation velocity experiment with a single protein solute , the sedimentation of the solute away from the ...
... meniscus between the solution and a heavy liquid that is added to the cell to give it a trans- parent bottom . In a typical sedimentation velocity experiment with a single protein solute , the sedimentation of the solute away from the ...
Page 6
... meniscus solute concentra- tion falls to zero and a widening zone of pure solvent extends from the meniscus . At distances further from the center of rotation than the zero concentration zone , the concentration rises smoothly to a zone ...
... meniscus solute concentra- tion falls to zero and a widening zone of pure solvent extends from the meniscus . At distances further from the center of rotation than the zero concentration zone , the concentration rises smoothly to a zone ...
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-ยน 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