title: Retention of native-like structure in an acyclic counterpart of a beta-sheet antibiotic.
abstract: An acyclic derivative of the cyclic peptide antibiotic, ramoplanin, has been prepared. In aqueous solution, two-dimensional NMR spectroscopy indicates that the acyclic form adopts a threshold population of conformers in which at least part of the beta-sheet characteristic of the intact ramoplanin persists. Thus, despite losing the entropic benefit which the macrocycle must lend to beta-sheet formation, the polypeptide chain of the acyclic ramoplanin appears to display an innate tendency to adopt a native-like conformation.
authors.affiliation: Cambridge Centre for Molecular Recognition, University Chemical Laboratory, UK.
authors.forename: R A
authors.initials: RA
authors.lastname: Maplestone
authors.forename: J P
authors.initials: JP
authors.lastname: Cox
authors.forename: D H
authors.initials: DH
authors.lastname: Williams
mesh_terms: D000900:Anti-Bacterial Agents / Q000737:chemistry*; D047630:Depsipeptides; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D010456:Peptides, Cyclic; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012995:Solubility; D012996:Solutions
chemical_list: D000900:Anti-Bacterial Agents; D047630:Depsipeptides; D010456:Peptides, Cyclic; D012996:Solutions; C041438:ramoplanin