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Science 23 May 1986:
Vol. 232. no. 4753, pp. 960 - 967
DOI: 10.1126/science.3518060
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Articles

Science, Vol 232, Issue 4753, 960-967
Copyright © 1986 by American Association for the Advancement of Science

articles

Two-dimensional nuclear magnetic resonance spectroscopy

A Bax and L Lerner

Great spectral simplification can be obtained by spreading the conventional one-dimensional nuclear magnetic resonance (NMR) spectrum in two independent frequency dimensions. This so-called two-dimensional NMR spectroscopy removes spectral overlap, facilitates spectral assignment, and provides a wealth of additional information. For example, conformational information related to interproton distances is available from resonance intensities in certain types of two-dimensional experiments. Another method generates 1H NMR spectra of a preselected fragment of the molecule, suppressing resonances from other regions and greatly simplifying spectral appearance. Two-dimensional NMR spectroscopy can also be applied to the study of 13C and 15N, not only providing valuable connectivity information but also improving sensitivity of 13C and 15N detection by up to two orders of magnitude.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy.
G. Clore and A. Gronenborn (1991)
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Protein carbon-13 spin systems by a single two-dimensional nuclear magnetic resonance experiment.
B. Oh, W. Westler, P Darba, and J. Markley (1988)
Science 240, 908-911
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