title: Protein conformational space populated in solution probed with aromatic residual dipolar (13) C-(1) H couplings.
abstract: The use of aromatic (13) C-(1) H residual dipolar couplings (RDCs) to probe the conformational space populated in solution is demonstrated for the protein BPTI. RDCs allow one to assess accuracy of atomic resolution structures and potentially to characterize low-populated subspaces corresponding to "excited states" in conformationally labile systems. They also allow one to assess sampling accuracy of molecular dynamics simulations.
authors.affiliation: Department of Chemistry, State University of New York at Buffalo, North Campus, Buffalo, NY 14260, USA.
authors.forename: Bharathwaj
authors.initials: B
authors.lastname: Sathyamoorthy
authors.forename: Kiran K
authors.initials: KK
authors.lastname: Singarapu
authors.forename: Angel E
authors.initials: AE
authors.lastname: Garcia
authors.forename: Thomas
authors.initials: T
authors.lastname: Szyperski
mesh_terms: D000818:Animals; D007611:Aprotinin / Q000737:chemistry*; D002417:Cattle; D056004:Molecular Dynamics Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D012996:Solutions
chemical_list: D012996:Solutions; D007611:Aprotinin