Effects of hydrogen bonding on amide-proton chemical shift anisotropy in a proline-containing model peptide

Kumar Pichumani, Gijo George, Sankeerth Hebbar, Bhaswati Chatterjee, Srinivasarao Raghothama

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Abstract Longitudinal relaxation due to cross-correlation between dipolar (1HN-1Hα) and amide-proton chemical shift anisotropy (1HN CSA) has been measured in a model tripeptide Piv-LPro-LPro-LPhe-OMe. The peptide bond across diproline segment is known to undergo cis/trans isomerization and only in the cis form does the lone Phe amide-proton become involved in intramolecular hydrogen bonding. The strength of the cross correlated relaxation interference is found to be significantly different between cis and trans forms, and this difference is shown as an influence of intramolecular hydrogen bonding on the amide-proton CSA.

Original languageEnglish (US)
Article number32894
Pages (from-to)126-129
Number of pages4
JournalChemical Physics Letters
Volume627
DOIs
StatePublished - May 1 2015

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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