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.
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
- No. of pages:
- © Academic Press 1994
- 1st September 1994
- Academic Press
- eBook ISBN:
- Hardcover ISBN:
@from:Praise for the Volume @qu:"Applications of high-resolution NMR techniques to biological systems have advances significantly since the publication of the two previous volumes in 1989. This book succeeds in covering these developments in an authoritative andcomprehensive manner... The serious investigator will be rewarded with an in-depth understanding of much that is important in modern protein NMR spectroscopy." @source:--ANALYTICAL BIOCHEMISTRY @from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for bioche