title: Interactive NMR and computer simulation studies of lanthionine-ring structures.
abstract: We report progress in elucidating the structure of nisin, a naturally occurring peptide antibiotic. Nisin contains five rings constrained by lanthionine or methyllanthionine bridges, as well as alpha, beta-unsaturated amino acids. We have determined conformations for two model compounds of ring A and a derivative of ring B through interactive nmr and computer simulation studies. High-resolution nmr techniques provides structural information, which was further refined through molecular dynamics simulations. These methods are being applied to the remaining constrained fragments of the molecule. This conformational information will be employed in an aufbau approach to determining the structure of the entire molecule.
authors.forename: D E
authors.initials: DE
authors.lastname: Palmer
authors.forename: D F
authors.initials: DF
authors.lastname: Mierke
authors.forename: C
authors.initials: C
authors.lastname: Pattaroni
authors.forename: M
authors.initials: M
authors.lastname: Goodman
authors.forename: T
authors.initials: T
authors.lastname: Wakamiya
authors.forename: K
authors.initials: K
authors.lastname: Fukase
authors.forename: M
authors.initials: M
authors.lastname: Kitazawa
authors.forename: H
authors.initials: H
authors.lastname: Fujita
authors.forename: T
authors.initials: T
authors.lastname: Shiba
mesh_terms: D000409:Alanine / Q000031:analogs & derivatives*; D000595:Amino Acid Sequence; D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009561:Nisin; D010456:Peptides, Cyclic; D011487:Protein Conformation; D013440:Sulfides
chemical_list: D010456:Peptides, Cyclic; D013440:Sulfides; D009561:Nisin; C001520:lanthionine; D000409:Alanine