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Science 13 May 1988:
Vol. 240. no. 4854, pp. 908 - 911
DOI: 10.1126/science.3129784
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Articles

Science, Vol 240, Issue 4854, 908-911
Copyright © 1988 by American Association for the Advancement of Science

articles

Protein carbon-13 spin systems by a single two-dimensional nuclear magnetic resonance experiment

BH Oh, WM Westler, P Darba, and JL Markley

Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison 53706.

By applying a two-dimensional double-quantum carbon-13 nuclear magnetic resonance experiment to a protein uniformly enriched to 26 percent carbon-13, networks of directly bonded carbon atoms were identified by virtue of their one-bond spin-spin couplings and were classified by amino acid type according to their particular single- and double-quantum chemical shift patterns. Spin systems of 75 of the 98 amino acid residues in a protein, oxidized Anabaena 7120 ferredoxin (molecular weight 11,000), were identified by this approach, which represents a key step in an improved methodology for assigning protein nuclear magnetic resonance spectra. Missing spin systems corresponded primarily to residues located adjacent to the paramagnetic iron-sulfur cluster.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution.
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Science 249, 411-414
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