ISBN-13: 978-0-12-164491-8 / ISBN-10: 0-12-164491-X / 885 pp.
Summary
Protein NMR Spectroscopy provides a complete introduction to solution NMR spectroscopy for determining three-dimensional structures, dynamical properties, and intermolecular interactions of proteins. The Second Edition of this now classic text provides an authoritative presentation of the theoretical principles and experimental practices required for the most sophisticated applications of solution NMR spectroscopy to explicate the molecular basis of protein function, which in turn is increasingly important for understanding mechanisms of disease and for developing novel therapeutic approaches
Key Features
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Bloch, density matrix and product operator theoretical formalisms
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One-, two-, three-, and four-dimensional NMR spectroscopy
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Semiclassical relaxation theory and chemical exchange effects
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Practical aspects of experimental NMR spectroscopy
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Proton homonuclear NMR experiments relevant for proteins and other biological macromolecules
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13C and 15N heteronuclear NMR experiments relevant for proteins and other biological macromolecules
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Extensive examples of NMR spectra for 1H, 15N,and 13C/15N proteins
Table of Contents
Errata
About the Authors
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Hierarchical links
Updated 10/6/07 by Arthur G. Palmer
(agp6@columbia.edu)
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