title: De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy.
abstract: The three-dimensional structure of the chemotactic peptide N-formyl-l-Met-l-Leu-l-Phe-OH was determined by using solid-state NMR (SSNMR). The set of SSNMR data consisted of 16 (13)C-(15)N distances and 18 torsion angle constraints (on 10 angles), recorded from uniformly (13)C,(15)N- and (15)N-labeled samples. The peptide's structure was calculated by means of simulated annealing and a newly developed protocol that ensures that all of conformational space, consistent with the structural constraints, is searched completely. The result is a high-quality structure of a molecule that has thus far not been amenable to single-crystal diffraction studies. The extensions of the SSNMR techniques and computational methods to larger systems appear promising.
authors.affiliation: Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
authors.forename: Chad M
authors.initials: CM
authors.lastname: Rienstra
authors.forename: Lisa
authors.initials: L
authors.lastname: Tucker-Kellogg
authors.forename: Christopher P
authors.initials: CP
authors.lastname: Jaroniec
authors.forename: Morten
authors.initials: M
authors.lastname: Hohwy
authors.forename: Bernd
authors.initials: B
authors.lastname: Reif
authors.forename: Michael T
authors.initials: MT
authors.lastname: McMahon
authors.forename: Bruce
authors.initials: B
authors.lastname: Tidor
authors.forename: Tomas
authors.initials: T
authors.lastname: Lozano-Pérez
authors.forename: Robert G
authors.initials: RG
authors.lastname: Griffin
mesh_terms: D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010455:Peptides / Q000737:chemistry; D017434:Protein Structure, Tertiary
chemical_list: D010455:Peptides; D009240:N-Formylmethionine Leucyl-Phenylalanine