title: Structural flexibility of Aib-containing peptides: the N-terminal tripeptide of trichotoxin.
abstract: The sequence Aib-Gly-Aib which corresponds to the N-terminus of the microheterogeneous peptide antibiotic trichotoxin has been studied crystallographically in the context of different protecting groups. Peptides Ac-Aib-Gly-Aib-OH (A) and Z-Aib-Gly-Aib-OH (B) form beta-turns. Both peptides show a remarkable conformational flexibility forming a large variety of beta-turns of different types.
authors.affiliation: Dept. of Biology, University of Crete, Greece.
authors.forename: R
authors.initials: R
authors.lastname: Gessmann
authors.forename: H
authors.initials: H
authors.lastname: Brueckner
authors.forename: M
authors.initials: M
authors.lastname: Kokkinidis
mesh_terms: D000595:Amino Acid Sequence; D000621:Aminoisobutyric Acids; D000900:Anti-Bacterial Agents / Q000737:chemistry; D023181:Antimicrobial Cationic Peptides; D003460:Crystallization; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation
chemical_list: D000621:Aminoisobutyric Acids; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D009842:Oligopeptides; D010455:Peptides; C016161:trichotoxin