High-Resolution 1H NMR Study of the Solution Structure of Alamethicin

Gennaro Esposito, John A. Carver, Jonathan Boyd, Iain D. Campbell

Research output: Contribution to journalArticle

Abstract

A 1H NMR study of the peptide alamethicin, which forms voltage-gated ion channels in membranes, is described. The molecule was studied in methanol as a function of temperature and pH. A complete assignment of the spectra is given, including several stereospecific assignments. Alamethicin was found to have a structure substantially similar to the crystal although, in solution, the C-terminal dipeptide adopts a somewhat extended conformation. The overall conformation was insensitive to the ionization of the side chain of the only ionizable group, Glu-18.

Original languageEnglish (US)
Pages (from-to)1043-1050
Number of pages8
JournalBiochemistry
Volume26
Issue number4
DOIs
StatePublished - Jan 1 1987

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Alamethicin
Conformations
Nuclear magnetic resonance
Dipeptides
Ion Channels
Ionization
Methanol
Membranes
Peptides
Crystals
Molecules
Temperature
Electric potential
Proton Magnetic Resonance Spectroscopy

ASJC Scopus subject areas

  • Biochemistry

Cite this

High-Resolution 1H NMR Study of the Solution Structure of Alamethicin. / Esposito, Gennaro; Carver, John A.; Boyd, Jonathan; Campbell, Iain D.

In: Biochemistry, Vol. 26, No. 4, 01.01.1987, p. 1043-1050.

Research output: Contribution to journalArticle

Esposito, Gennaro ; Carver, John A. ; Boyd, Jonathan ; Campbell, Iain D. / High-Resolution 1H NMR Study of the Solution Structure of Alamethicin. In: Biochemistry. 1987 ; Vol. 26, No. 4. pp. 1043-1050.
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