Protein structure determination by combining sparse NMR data with evolutionary couplings

Yuefeng Tang, Yuanpeng Janet Huang, Thomas A. Hopf, Chris Sander, Debora S. Marks, Gaetano T. Montelione

Research output: Contribution to journalArticle

47 Citations (Scopus)

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 6â '41 kDa in size.

Original languageEnglish (US)
Pages (from-to)751-754
Number of pages4
JournalNature Methods
Volume12
Issue number8
DOIs
StatePublished - Jul 30 2015

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Nuclear magnetic resonance
Biomolecular Nuclear Magnetic Resonance
Nuclear magnetic resonance spectroscopy
Entropy
Proteins
Magnetic Resonance Spectroscopy
Statistical methods

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Tang, Yuefeng ; Huang, Yuanpeng Janet ; Hopf, Thomas A. ; Sander, Chris ; Marks, Debora S. ; Montelione, Gaetano T. / Protein structure determination by combining sparse NMR data with evolutionary couplings. In: Nature Methods. 2015 ; Vol. 12, No. 8. pp. 751-754.
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Protein structure determination by combining sparse NMR data with evolutionary couplings. / Tang, Yuefeng; Huang, Yuanpeng Janet; Hopf, Thomas A.; Sander, Chris; Marks, Debora S.; Montelione, Gaetano T.

In: Nature Methods, Vol. 12, No. 8, 30.07.2015, p. 751-754.

Research output: Contribution to journalArticle

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