Cyclized dipeptide model for a β-bend Academic Article Article uri icon


MeSH Major

  • Carrier Proteins
  • Membrane Glycoproteins
  • Membrane Transport Proteins
  • Sterols


  • A cyclic dipeptide in which L-Ala-Gly was cyclized with epsilon-aminocaproic acid has been synthesized as a model for a beta-bend. Its conformational properties have been examined by means of conformational energy calculations and nuclear magnetic resonance, infrared, Raman, and circular dichroism spectroscopy in various solvents. These calculations and experiments suggest that a type II beta-bend exists in the Ala-Glymoiety, with an NH...O = C hydrogen bond in the epsilon-aminocaproic acid portion of the molecule, and that the molecule adopts a unique conformation in solution. In contrast, an open-chain analog of this compound exists in solution as an ensemble of conformations but with a significant amount of a type II beta-bend structure in the ensemble.

publication date

  • November 2, 1979



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1073/pnas.76.6.2512

PubMed ID

  • 288041

Additional Document Info

start page

  • 2512

end page

  • 4


  • 76


  • 6