CONFORMATIONS OF PROLINE‐CONTAINING CYCLIC PEPTIDES: 1H and 13C n.m.r. Evidence for a Solvent Stabilized All‐Cis X‐Pro Conformer of Cyclo‐(Pro‐Gly‐Gly‐Pro)2

M. Hollosi, L. Radics, Th Wieland

Research output: Contribution to journalArticle

11 Citations (Scopus)


As inferred from 13C, 1H n.m.r. data, CD measurements and ion‐binding experiments, the title molecule can assume two major C2 symmetric conformations. One of these has an all‐trans X‐Pro peptide backbone with two 1 4 intramolecular H‐bonds and represents the predominant (≥ 95%) form in D2O and nonpolar (CD3CN) solvents. Stabilized by specific solvent‐solute interactions, the other conformer becomes competitive (45%) in DMSO solution. It is shown to possess a four‐cis X‐Pro skeleton and no intramolecular H‐bonds. The Mg++ complex of the cyclic peptide in CD3CN is again C2 symmetric and its formation proceeds via a slow trans → cis isomerization of two X‐Pro peptide bonds.

Original languageEnglish
Pages (from-to)286-290
Number of pages5
JournalInternational journal of peptide and protein research
Issue number4
Publication statusPublished - Oct 1977


  • proline peptides‐cyclic peptides‐prolin‐C‐nmr‐ring‐conformation‐complexones

ASJC Scopus subject areas

  • Biochemistry

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