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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.
Afiliación
  • Tang Y; 1] Center for Advanced Biotechnology and Medicine, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA. [2] Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA.
  • Huang YJ; 1] Center for Advanced Biotechnology and Medicine, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA. [2] Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA.
  • Hopf TA; 1] Department of Systems Biology, Harvard Medical School, Boston, Massachusetts, USA. [2] Department of Informatics, Technische Universität München, Garching, Germany.
  • Sander C; Computational Biology Center, Memorial Sloan Kettering Cancer Center, New York, New York, USA.
  • Marks DS; Department of Systems Biology, Harvard Medical School, Boston, Massachusetts, USA.
  • Montelione GT; 1] Center for Advanced Biotechnology and Medicine, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA. [2] Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA. [3] Department of Biochemistry and Molecular Bi
Nat Methods ; 12(8): 751-4, 2015 Aug.
Article en En | MEDLINE | ID: mdl-26121406
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Espectroscopía de Resonancia Magnética / Proteínas / Biología Computacional Tipo de estudio: Risk_factors_studies Límite: Humans Idioma: En Revista: Nat Methods Asunto de la revista: TECNICAS E PROCEDIMENTOS DE LABORATORIO Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Espectroscopía de Resonancia Magnética / Proteínas / Biología Computacional Tipo de estudio: Risk_factors_studies Límite: Humans Idioma: En Revista: Nat Methods Asunto de la revista: TECNICAS E PROCEDIMENTOS DE LABORATORIO Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos