| Literature DB >> 23851009 |
Abstract
An assignment of the helical hairpin of the influenza fusion peptide has been made based on the hydrophobic moments, represented in a form of two-dimensional map. Such assignment holds for all serotypes, even for the cases of mutations altering the amino acid character. Similar results are obtained for the experimentally developed hydrophobicity scales, whose values reflect the transfer energies between aqueous and membrane environments. A distinct, however still structure-related hydrophobic map corresponds to a helical and contiguous HIV gp41 fp. The method may be used as a simple tool for sequence-based prediction of structures adopted by viral fusion peptides.Keywords: Amphiphilic helix; HAfp; Hydrophobic moment; Influenza virus; Membrane fusion; Sequence analysis; fp; fusion peptide; hemagglutinin fusion peptide; mean hydrophobic moment; 〈μ(H)〉
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Year: 2013 PMID: 23851009 DOI: 10.1016/j.febslet.2013.06.054
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124