Figure 2.

The transmembrane region of influenza virus HA contains a groove that might accommodate a fatty acid

Hydrophobic/hydrophilic properties (left panel) and landscape (right panel) of the solvent‐accessible surface of the transmembrane region helix of influenza A virus hemagglutinin (HA). Surfaces are projected onto a cylinder and shown as 2D maps (angle of rotation along the helical axis and rise along it). Hydrophobic/hydrophilic properties are mapped on the surface according to molecular hydrophobicity potential (MHP) approach and expressed in water–octanol logP units. Maps are coloured according to the scales given below. The hydrophilic groove composed of Ala 20, Gly 16 and Ser 9 could accommodate the acyl chain of a fatty acid attached to Cys 26. The peptide NH2‐ILAIYSTVSSSLVLVGLIIAVGLWMC‐COOH, corresponding to the TMR of H6‐subtype HA, was used for the analysis, which was performed by Anton Polyansky (Shemyakin‐Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow).

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