Protein Carbon-13 Spin Systems by a Single Two-Dimensional Nuclear Magnetic Resonance Experiment
- 13 May 1988
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 240 (4854) , 908-911
- https://doi.org/10.1126/science.3129784
Abstract
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.Keywords
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