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The secondary structure of influenza A M2 transmembrane domain. A circular dichroism study
K C Duff1, S M Kelly, N C Price
1Department of Biochemistry, University of Edinburgh Medical School, Scotland, UK.
FEBS Letters
|October 26, 1992
Abstract:
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 alpha-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.