Protein structure determination by combining sparse NMR data with evolutionary couplings

Accurate protein structure determination by NMR is challenging for larger proteins, for which experimental data is often incomplete and ambiguous. Fortunately, the upsurge in evolutionary sequence information and advances in maximum entropy statistical methods now provide a rich complementary source...

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Autores principales: Tang, Yuefeng, Huang, Yuanpeng Janet, Hopf, Thomas A., Sander, Chris, Marks, Debora S., Montelione, Gaetano T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4521990/
https://www.ncbi.nlm.nih.gov/pubmed/26121406
http://dx.doi.org/10.1038/nmeth.3455
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author Tang, Yuefeng
Huang, Yuanpeng Janet
Hopf, Thomas A.
Sander, Chris
Marks, Debora S.
Montelione, Gaetano T.
author_facet Tang, Yuefeng
Huang, Yuanpeng Janet
Hopf, Thomas A.
Sander, Chris
Marks, Debora S.
Montelione, Gaetano T.
author_sort Tang, Yuefeng
collection PubMed
description Accurate protein structure determination by NMR is challenging for larger proteins, for which experimental data is often incomplete and ambiguous. Fortunately, the upsurge in evolutionary sequence information and advances in maximum entropy statistical methods now provide a rich complementary source of structural constraints. We have developed a hybrid approach (EC-NMR) combining sparse NMR data with evolutionary residue-residue couplings, and demonstrate accurate structure determination for several 6 to 41 kDa proteins.
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spelling pubmed-45219902016-01-31 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. Nat Methods Article Accurate protein structure determination by NMR is challenging for larger proteins, for which experimental data is often incomplete and ambiguous. Fortunately, the upsurge in evolutionary sequence information and advances in maximum entropy statistical methods now provide a rich complementary source of structural constraints. We have developed a hybrid approach (EC-NMR) combining sparse NMR data with evolutionary residue-residue couplings, and demonstrate accurate structure determination for several 6 to 41 kDa proteins. 2015-06-29 2015-08 /pmc/articles/PMC4521990/ /pubmed/26121406 http://dx.doi.org/10.1038/nmeth.3455 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
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
title Protein structure determination by combining sparse NMR data with evolutionary couplings
title_full Protein structure determination by combining sparse NMR data with evolutionary couplings
title_fullStr Protein structure determination by combining sparse NMR data with evolutionary couplings
title_full_unstemmed Protein structure determination by combining sparse NMR data with evolutionary couplings
title_short Protein structure determination by combining sparse NMR data with evolutionary couplings
title_sort protein structure determination by combining sparse nmr data with evolutionary couplings
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4521990/
https://www.ncbi.nlm.nih.gov/pubmed/26121406
http://dx.doi.org/10.1038/nmeth.3455
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