Molecular structure of peptaibol antibiotics: solution conformation and crystal structure of the octapeptide corresponding to the 2-9 sequence of emerimicins III and IV

J Biomol Struct Dyn. 1985 Dec;3(3):585-98. doi: 10.1080/07391102.1985.10508446.

Abstract

The infrared absorption and 1H nuclear magnetic resonance analyses of chloroform solutions of the terminally-blocked segment corresponding to the 2-9 sequence of emerimicins III and IV, -(Aib)3-L-Val-Gly-L-Leu-(Aib)2-, are consistent with the presence of a 3(10)-helical structure of high thermal stability. The crystal structure of the octapeptide, obtained by X-ray diffraction indicates the formation of a right-handed 3(10)-helix, stabilized by six consecutive intramolecular N-H....O:C H-bonds, slightly distorted at the level of the L-Leu residue.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents*
  • Molecular Sequence Data
  • Molecular Structure
  • Oligopeptides
  • Peptaibols
  • Peptides*
  • Protein Conformation

Substances

  • Anti-Bacterial Agents
  • Oligopeptides
  • Peptaibols
  • Peptides