Laboratory of Biological Physics, Institute of Physics, Polish Academy of Sciences, Warsaw 02-668, Poland.
FEBS Lett. 2013 Sep 17;587(18):2980-3. doi: 10.1016/j.febslet.2013.06.054. Epub 2013 Jul 11.
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.
已根据疏水性矩（以二维图谱的形式表示）对流感融合肽的螺旋发夹进行了分配。这种分配适用于所有血清型，即使是改变氨基酸特征的突变情况也是如此。对于实验开发的疏水性标度，也得到了类似的结果，其值反映了在水相和膜环境之间的转移能量。一个独特的、但仍然与结构相关的疏水性图谱对应于螺旋且连续的 HIV gp41 fp。该方法可用作基于序列预测病毒融合肽所采用结构的简单工具。
