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 87
Page 10
... Section VII . Many proteins are studied under conditions where they carry an elec- tric charge . To minimize the effect of this charge on sedimentation be- havior , a salt ( alone , or together with a weak acid or base to buffer the pH ...
... Section VII . Many proteins are studied under conditions where they carry an elec- tric charge . To minimize the effect of this charge on sedimentation be- havior , a salt ( alone , or together with a weak acid or base to buffer the pH ...
Page 11
... Section VII . B. SEDIMENTATION EQUILIBRIUM 1. Two - Component Systems : Solvent and a Single Solute In a sedimentation equilibrium experiment , a protein solution is sub- ject to a centrifugal field such that the rate of sedimentation ...
... Section VII . B. SEDIMENTATION EQUILIBRIUM 1. Two - Component Systems : Solvent and a Single Solute In a sedimentation equilibrium experiment , a protein solution is sub- ject to a centrifugal field such that the rate of sedimentation ...
Page 14
... section will not apply as it stands , since it assumed that the chemical potential of the protein solute is de- termined solely by its own concentration . The work of Scatchard ( 1946 ) and Casassa and Eisenberg ( 1960 , 1961 , 1964 ) ...
... section will not apply as it stands , since it assumed that the chemical potential of the protein solute is de- termined solely by its own concentration . The work of Scatchard ( 1946 ) and Casassa and Eisenberg ( 1960 , 1961 , 1964 ) ...
Page 17
... Section II , B , 2 , the protein component whose molecular weight is measured is implicitly defined by the way in which the density increment is measured . Furthermore , if refractive index measurements are used to determine the protein ...
... Section II , B , 2 , the protein component whose molecular weight is measured is implicitly defined by the way in which the density increment is measured . Furthermore , if refractive index measurements are used to determine the protein ...
Page 20
... Section II , D , 3 , a . e . Materials Used for Cell Centerpieces . The ideal centerpiece material should be rigid , hard , easily machined , chemically inert , and form a leak- proof seal to quartz windows without the use of gaskets ...
... Section II , D , 3 , a . e . Materials Used for Cell Centerpieces . The ideal centerpiece material should be rigid , hard , easily machined , chemically inert , and form a leak- proof seal to quartz windows without the use of gaskets ...
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