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.
authors.affiliation: 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.
authors.forename: Yuefeng
authors.initials: Y
authors.lastname: Tang
authors.affiliation: 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.
authors.forename: Yuanpeng Janet
authors.initials: YJ
authors.lastname: Huang
authors.affiliation: 1] Department of Systems Biology, Harvard Medical School, Boston, Massachusetts, USA. [2] Department of Informatics, Technische Universität München, Garching, Germany.
authors.forename: Thomas A
authors.initials: TA
authors.lastname: Hopf
authors.affiliation: Computational Biology Center, Memorial Sloan Kettering Cancer Center, New York, New York, USA.
authors.forename: Chris
authors.initials: C
authors.lastname: Sander
authors.affiliation: Department of Systems Biology, Harvard Medical School, Boston, Massachusetts, USA.
authors.forename: Debora S
authors.initials: DS
authors.lastname: Marks
authors.affiliation: 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 Biology, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA.
authors.forename: Gaetano T
authors.initials: GT
authors.lastname: Montelione
mesh_terms: D000465:Algorithms; D019295:Computational Biology / Q000379:methods*; D018360:Crystallography, X-Ray; D019143:Evolution, Molecular; D006801:Humans; D057446:Hydrodynamics; D021621:Imaging, Three-Dimensional; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D015233:Models, Statistical; D008968:Molecular Conformation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D011518:Proto-Oncogene Proteins / Q000737:chemistry; D016283:Proto-Oncogene Proteins p21(ras); D018631:ras Proteins / Q000737:chemistry
chemical_list: C117307:KRAS protein, human; D011506:Proteins; D011518:Proto-Oncogene Proteins; D016283:Proto-Oncogene Proteins p21(ras); D018631:ras Proteins