LONG RANGE HYDROGEN BOND MEDIATED EFFECTS IN PEPTIDES: **1**5N NMR STUDY OF GRAMICIDIN S IN WATER AND ORGANIC SOLVENTS.

David H. Live, Donald G. Davis, David Cowburn, David Cowburn

Research output: Contribution to journalArticle

231 Citations (Scopus)

Abstract

The chemical shifts of the **1**5Ns 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 **1**5N 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 **1**5N 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
StatePublished - Apr 4 1984
Externally publishedYes

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Gramicidin
Organic solvents
Peptides
Hydrogen
Hydrogen bonds
Nuclear magnetic resonance
Water
Cyclic Peptides
Chemical shift
Polarization
Temperature

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

LONG RANGE HYDROGEN BOND MEDIATED EFFECTS IN PEPTIDES : **1**5N NMR STUDY OF GRAMICIDIN S IN WATER AND ORGANIC SOLVENTS. / Live, David H.; Davis, Donald G.; Cowburn, David; Cowburn, David.

In: Journal of the American Chemical Society, Vol. 106, No. 7, 04.04.1984, p. 1939-1941.

Research output: Contribution to journalArticle

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