The secondary structure of influenza A M2 transmembrane domain A circular dichroism study
- 26 October 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 311 (3) , 256-258
- https://doi.org/10.1016/0014-5793(92)81114-2
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.Keywords
This publication has 23 references indexed in Scilit:
- Influenza virus M2 protein has ion channel activityPublished by Elsevier ,1992
- Emergence and Transmission of Influenza A Viruses Resistant to Amantadine and RimantadinePublished by Springer Nature ,1992
- Nuclear transport of influenza virus ribonucleoproteins: The viral matrix protein (M1) promotes export and inhibits importCell, 1991
- Detergent structure in crystals of a bacterial photosynthetic reaction centreNature, 1989
- Modulation of membrane surface curvature by peptide-lipid interactionsBioscience Reports, 1988
- Functional reconstitution of the integral membrane proteins of influenza virus into phospholipid liposomesBiochemistry, 1987
- Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolutionNature, 1985
- Amphipathic helix and its relationship to the interaction of calcitonin with phospholipidsBiochemistry, 1983
- Estimation of globular protein secondary structure from circular dichroismBiochemistry, 1981
- Circular dichroic analysis of protein conformation: Inclusion of the β-turnsAnalytical Biochemistry, 1978