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PMID: 1397324 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 311 ·No. 3 ·1992-10-26 ·Pages 256-8

Duff KC, Kelly SM, Price NC, Bradshaw JP

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.

MeSH Terms
Amantadine Amino Acid Sequence Circular Dichroism Indicators and Reagents Influenza A virus/chemistry Liposomes Molecular Sequence Data Peptides/chemical synthesis,chemistry Phosphatidylcholines Phosphatidylglycerols Protein Conformation Viral Matrix Proteins/chemistry
Chemicals
Indicators and Reagents Liposomes M-protein, influenza virus M2 protein, Influenza A virus Peptides Phosphatidylcholines Phosphatidylglycerols Viral Matrix Proteins 1,2-dioleoyl-sn-glycero-3-phosphoglycerol Amantadine 1,2-oleoylphosphatidylcholine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Duff K C
Department of Biochemistry, University of Edinburgh Medical School, Scotland, UK.
Kelly S M
Price N C
Bradshaw J P
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1992-10-26
Pages
256-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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