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 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 language | English |
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Pages (from-to) | 256-258 |
Number of pages | 3 |
Journal | FEBS Letters |
Volume | 311 |
Issue number | 3 |
DOIs | |
Publication status | Published - 26 Oct 1992 |
Keywords
- Circular dichroism
- Influenza M2 protein
- Ion channel
- Spectrophotometry
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology