The secondary structure of influenza A M2 transmembrane domain. A circular dichroism study.
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.
Duff
K C
KC
Department of Biochemistry, University of Edinburgh Medical School, Scotland, UK.
Kelly
S M
SM
Price
N C
NC
Bradshaw
J P
JP
D000547:Amantadine; D000595:Amino Acid Sequence; D002942:Circular Dichroism; D007202:Indicators and Reagents; D009980:Influenza A virus / Q000737:chemistry*; D008081:Liposomes; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry; D010713:Phosphatidylcholines; D010715:Phosphatidylglycerols; D011487:Protein Conformation; D014763:Viral Matrix Proteins / Q000737:chemistry*; D000086082:Viroporin Proteins
D000547:Amantadine; D007202:Indicators and Reagents; D008081:Liposomes; D010455:Peptides; D010713:Phosphatidylcholines; D010715:Phosphatidylglycerols; D014763:Viral Matrix Proteins; C031540:M-protein, influenza virus; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins; C051388:1,2-dioleoyl-sn-glycero-3-phosphoglycerol; C017251:1,2-oleoylphosphatidylcholine