Long Range Hydrogen Bond Mediated Effects in Peptides: 15N NMR Study of Gramicidin S in Water and Organic Solvents

David H. Live, William C. Agosta, David Cowburn, Donald G. Davis

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Abstract

The chemical shifts of the 15N's of the cyclic peptide gramicidin S in dilute aqueous solution were measured and assigned with use of polarization transfer via scalar coupling (INEPT). Long-range perturbations were detected in the 15N spectrum from comparison of these results and those in organic solvents. The effects are transmitted from one peptide linkage to another via an intramolecular hydrogen bond across a total of six bonds. The variation with temperature of the 15N shifts in these solvents further corroborates the roles of the intramolecular hydrogen bond in the propagation of shift effects. From the long-range effects it is possible to examine the relationship between solvent-peptide interactions and the properties of internal hydrogen bonds.

Original languageEnglish (US)
Pages (from-to)1939-1941
Number of pages3
JournalJournal of the American Chemical Society
Volume106
Issue number7
DOIs
Publication statusPublished - Jan 1 1984
Externally publishedYes

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ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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