Protein structure determination by combining sparse NMR data with evolutionary couplings Journal Article


Authors: Tang, Y.; Huang, Y. J.; Hopf, T. A.; Sander, C.; Marks, D. S.; Montelione, G. T.
Article Title: Protein structure determination by combining sparse NMR data with evolutionary couplings
Abstract: Accurate determination of protein structure by NMR spectroscopy is challenging for larger proteins, for which experimental data are often incomplete and ambiguous. Evolutionary sequence information together with advances in maximum entropy statistical methods provide a rich complementary source of structural constraints. We have developed a hybrid approach (evolutionary coupling-NMR spectroscopy; EC-NMR) combining sparse NMR data with evolutionary residue-residue couplings and demonstrate accurate structure determination for several proteins 6-41 kDa in size. © 2015 Nature America, Inc. All rights reserved.
Keywords: protein domain; protein analysis; amino acid sequence; nuclear magnetic resonance spectroscopy; protein structure; protein determination; proton transport; priority journal; article
Journal Title: Nature Methods
Volume: 12
Issue: 8
ISSN: 1548-7091
Publisher: Nature Publishing Group  
Date Published: 2015-08-01
Start Page: 751
End Page: 754
Language: English
DOI: 10.1038/nmeth.3455
PROVIDER: scopus
PMCID: PMC4521990
PUBMED: 26121406
DOI/URL:
Notes: Export Date: 2 September 2015 -- Source: Scopus
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  1. Chris Sander
    210 Sander