Spectroscopic study of the conformations of proline-containing oligopeptides in the crystalline state and in solution. Academic Article uri icon


MeSH Major

  • Oligopeptides
  • Proline


  • A conformational study has been carried out on a series of linear proline-containing oligopeptides (ZGP, ZGPL, ZGPLG and ZGPLGP) in both the crystalline state and in DMSO-d6 solution, using Raman and n.m.r. spectroscopy. The amide I and III bands in the Raman spectra of the crystalline forms indicate the presence of the type I beta-bend conformation in ZGPLG and ZGPLGP, but not in ZGP and ZGPL. This result is in agreement with X-ray data on these molecules. The Raman spectra of these peptides in solution indicate that more than one conformation is present, i.e. that the beta-bend structure of the solid form of ZGPLG and ZGPLGP is destabilized by DMSO-d6. 13C and 1H n.m.r. data also demonstrate the presence of more than one conformation in ZGP, ZGPL, ZGPLG and ZGPLGP in DMSO-d6 solution. These isomers differ in their conformation (cis and trans) about their Gly-Pro peptide bonds and possibly about the c alpha-C' bond of the C-terminal proline in ZGPLGP. For ZGP, ZGPL, ZGPLG and ZGPLGP, the ensemble of conformations in DMSO-d6 includes C5 and C7 hydrogen-bonded rings; in addition, ZGPLGP may contain a small percentage of a beta-bend conformation (at Pro2-Leu3) with trans peptides in both Gly-Pro moieties.

publication date

  • March 1981



  • Academic Article



  • eng

PubMed ID

  • 7287301

Additional Document Info

start page

  • 297

end page

  • 315


  • 17


  • 3