title: 1H NMR study on the conformation of bacitracin A in aqueous solution.
abstract: The conformation of bacitracin A, a widely used cyclic dodecapeptide antibiotic in aqueous solution, has been investigated using 500 MHz 1H NMR and molecular modeling. Findings revealed that a region (residues 1-6) is folded over the cyclic ring, resulting in metal coordination sites, a thiazoline ring, and Glu4 and His10 being proximate to each other.
authors.affiliation: Institute of Applied Biochemistry, University of Tsukuba, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Kobayashi
authors.forename: T
authors.initials: T
authors.lastname: Takenouchi
authors.forename: S
authors.initials: S
authors.lastname: Endo
authors.forename: E
authors.initials: E
authors.lastname: Munekata
mesh_terms: D000595:Amino Acid Sequence; D001414:Bacitracin / Q000031:analogs & derivatives* / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D001414:Bacitracin; C026461:bacitracin A