title: The helical hairpin structure of the influenza fusion peptide can be seen on a hydrophobic moment map.
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.
authors.affiliation: Laboratory of Biological Physics, Institute of Physics, Polish Academy of Sciences, Warsaw 02-668, Poland. remiwo@ifpan.edu.pl
authors.forename: Remigiusz
authors.initials: R
authors.lastname: Worch
mesh_terms: D020816:Amino Acid Motifs; D015700:HIV Envelope Protein gp41 / Q000737:chemistry*; D006389:Hemagglutinins, Viral / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D017433:Protein Structure, Secondary; D014760:Viral Fusion Proteins / Q000737:chemistry*
chemical_list: D015700:HIV Envelope Protein gp41; D006389:Hemagglutinins, Viral; D014760:Viral Fusion Proteins; C458881:hemagglutinin fusogenic peptide, influenza virus
keywords: Amphiphilic helix; HAfp; Hydrophobic moment; Influenza virus; Membrane fusion; Sequence analysis; fp; fusion peptide; hemagglutinin fusion peptide; mean hydrophobic moment; 〈μ(H)〉