Protein NMR Spectroscopy. Principles and Practice

This is the legacy WWW site for the First Edition of Protein NMR Spectroscopy. The Second Edition of Protein NMR Spectroscopy is now available

ISBN: 0-12-164490-1 / 587 pp. / hardcover

Summary

Protein NMR Spectroscopy combines a comprehensive theoretical treatment of high resolution NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments. Protein NMR Spectroscopy is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or who wish to understand the latest developments in this important field.

Key Features

Bloch, density matrix and product operator theoretical formalisms
One-, two-, three-, and four-dimensional NMR spectroscopy
Semiclassical relaxation theory and chemical exchange effects
Practical aspects of experimental NMR spectroscopy
Proton homonuclear NMR experiments relevant for proteins and other biological macromolecules
13C and 15N heteronuclear NMR experiments relevant for proteins and other biological macromolecules
Extensive examples of NMR spectra for 1H, 15N,and 13C/15N proteins

Table of Contents

Errata

About the Authors

John Cavanagh is at the Wadsworth Center for Laboratories & Research, New York State Department of Health and State University of New York at Albany.
Wayne Fairbrother and Nicholas Skelton are in the Department of Protein Engineering at Genentech, Inc..
Arthur G. Palmer is in the Department of Biochemistry and Molecular Biophysics, Columbia University.

Hierarchical links

Updated 7/23/99 by Arthur G. Palmer (agp6@columbia.edu)