Nuclear Magnetic Resonance Spectroscopy is the only "tool" available for the determination of high-resolution biological molecule structure in solution. This volume includes methods for expeditiously analyzing the vast amount of data produced by the new 3D and 4D NMR techniques and for generating structures from the data and for assessing the quality of those structures. Application to various classes of important proteins and protein-ligand complexes illustrate uses of the methodology presented. Examination of techniques to explore the dynamic nature of proteins complete the volume.


Biochemists, organic chemists, analytical chemists, biophysicists, drug company researchers.

Table of Contents

Techniques: A. Experimentation: A.S. Edison, F. Abildgaard, W.M. Westler, E.S. Mooberry, and J.L. Markley, Practical Introduction to Theory and Implementation of Multinuclear, Multidimensional Nuclear Magnetic Resonance Experiments. G.W. Vuister, S. Grzesiek, F. Delaglio, A.C. Wang, R. Tschudin, G. Zhu, and A. Bax, Measurement of Homo- and Heteronuclear J Couplings from Quantitative J Correlation. S.I. Macura, W.M. Westler, and J.L. Markley, Two-Dimensional Exchange Spectroscopy of Proteins. J. Keeler, R.T. Clowes, A.L. Davis, and E.D. Laue, Pulsed-Field Gradients: Theory and Practice. L. Emsley, Selective Pulses and Their Applications to Assignment and Structure Determination in Nuclear Magnetic Resonance. E.S. Mooberry, F. Abildgaard, and J.L. Markley, Modifications of Older Model Nuclear Magnetic Resonance Console for Collection of Multinuclear, Multidimensional Spectral Data. B. Data Processing: P.N. Borer and G.C. Levy, Using Maximum Likelihood Spectral Deconvolution in Multidimensional Nuclear Magnetic Resonance. M. Kjaer, K.V. Andersen, and F.M. Poulsen, Automated and Semiautomated Analysis of Homo- and Heteronuclear Multidimensional Nuclear Magnetic Resonance Spectra of Proteins: The Program Pronto. H. Oschkinat and D. Croft, Automated Assignment of Multidimensional Nuclear Magnetic Resonance Spectra. J.J. Led and H. Gesmar, Quantitative Information from Complicated Nuclear Magnetic Resonance Spectra of Biological Macromolecules. Protein Structure: A. General: G.M. Clore and A.M. Gronenborn, Multidimensional Heteronuclear Nuclear Magnetic Resonance of Proteins. D.S. Wishart and B.D. Sykes, Chemical Shifts


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© 1994
Academic Press
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