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Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2
1987
Journal of Biological Chemistry
Synthetic peptides representing amino acid residues 1-16 and 1-20, a proposed fusogenic region of the HA-2 subunit of influenza virus hemagglutinin, bind to phosphatidylcholine vesicles with submicromolar dissociation constants. The 1-20, but not the 1-16, peptide appears to adopt a helical conformation when bound to vesicles and cooperatively promotes vesicle fusion.
doi:10.1016/s0021-9258(18)48270-1
fatcat:xggmtlnlr5gbtonedwayao3upa