Protein structure determination by combining sparse NMR data with evolutionary couplings.
basic_science · Level V
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- Record sourced from PubMed, PMID 26121406.
- Also identified by DOI 10.1038/nmeth.3455 and PMC identifier 4521990.
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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.
Medical subject headings
- Computational Biology
- Magnetic Resonance Spectroscopy
- Proteins