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 journalArticlepeer-review

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 - 1987

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'High-Resolution <sup>1</sup>H NMR Study of the Solution Structure of Alamethicin'. Together they form a unique fingerprint.

Cite this