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Intramolecular interactions in protonated peptides: H+ PheGlyGly and H+ GlyGlyPhe.

PubMed
Authors: Vaden TD, de Boer TS, Simons JP, Snoek LC

Year

2008

Paper ID

12623

Status

Peer-reviewed

Abstract Read

~2 min

Abstract Words

97

Citations

40

Abstract

The conformations of protonated PheGlyGly and GlyGlyPhe tripeptides, generated at temperatures approximately 300-350 K through a photochemical mechanism, were investigated in the gas phase using R-IRMPD spectroscopy in the OH and NH stretch region in combination with quantum chemistry calculations. The results aid characterisation of their conformational landscapes and specifically, help identify the intramolecular interactions that control the peptide conformations. The dominant intramolecular interaction in protonated PheGlyGly operates between the N-and C-termini but in protonated GlyGlyPhe there is a strong cation-pi interaction. The observation of a cation-pi interaction in the warm ions highlights its strong, stable nature.

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  • The conformations of protonated PheGlyGly and GlyGlyPhe tripeptides, generated at temperatures approximately 300-350 K through a photochemical mechanism, were investigated in...

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References & Citation Signals

[1] DOI https://doi.org/10.1039/b716666d [2] Publisher https://pubmed.ncbi.nlm.nih.gov/18309401/

Local Citation Graph (Related-Paper Links)

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External citation index: OpenAlex citation signal • updated 2026-06-11 05:06:59

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