The secondary structure of influenza A M2 transmembrane domain A circular dichroism study

Kevin C. Duff, Sharon M. Kelly, Nicholas C. Price, Jeremy P. Bradshaw

Research output: Contribution to journalArticle


Using circular dichroism, this study investigated the secondary structure of the influenza A M2 transmembrane domain. When reconstituted into 1,2-dioleoyl-sn-glycero-3-phosphocholine liposomes, the M2 transmembrane domain was found to adopt a predominantly α-helical secondary structure which was unaffected by both temperature and the addition of 1-aminoadamantane hydrochloride. Reconstitution into 1,2-dioleoyl-sn-glycero-3-phosphoglycerol liposomes resulted in a marked decrease in helical content.

Original languageEnglish
Pages (from-to)256-258
Number of pages3
JournalFEBS Letters
Issue number3
Publication statusPublished - 26 Oct 1992


  • Circular dichroism
  • Influenza M2 protein
  • Ion channel
  • Spectrophotometry

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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