Structural flexibility of Aib-containing peptides: the N-terminal tripeptide of trichotoxin.
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.
Gessmann
R
R
Dept. of Biology, University of Crete, Greece.
Brueckner
H
H
Kokkinidis
M
M
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
D000621:Aminoisobutyric Acids; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D009842:Oligopeptides; D010455:Peptides; C016161:trichotoxin