tetano
Editor, Senior Moderator
FEBS Lett. 2013 Jul 10. pii: S0014-5793(13)00515-2. doi: 10.1016/j.febslet.2013.06.054. [Epub ahead of print]
The helical hairpin structure of the influenza fusion peptide can be seen on a hydrophobic moment map.
Worch R.
Source
Laboratory of Biological Physics, Institute of Physics, Polish Academy of Sciences, Warsaw 02-668, Poland. Electronic address: remiwo@ifpan.edu.pl.
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 fusion peptide. The method may be used as a simple tool for sequence-based prediction of structures adopted by viral fusion peptides.
Copyright ? 2013. Published by Elsevier B.V.
KEYWORDS:
<(H)>, HAfp, amphiphilic helix, fp, fusion peptide, hemagglutinin fusion peptide, hydrophobic moment, influenza virus, mean hydrophobic moment, membrane fusion, sequence analysis
PMID:
23851009
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23851009
The helical hairpin structure of the influenza fusion peptide can be seen on a hydrophobic moment map.
Worch R.
Source
Laboratory of Biological Physics, Institute of Physics, Polish Academy of Sciences, Warsaw 02-668, Poland. Electronic address: remiwo@ifpan.edu.pl.
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 fusion peptide. The method may be used as a simple tool for sequence-based prediction of structures adopted by viral fusion peptides.
Copyright ? 2013. Published by Elsevier B.V.
KEYWORDS:
<(H)>, HAfp, amphiphilic helix, fp, fusion peptide, hemagglutinin fusion peptide, hydrophobic moment, influenza virus, mean hydrophobic moment, membrane fusion, sequence analysis
PMID:
23851009
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23851009