Abstract
Hydrophobins are a family of proteins characterized by a large exposed hydrophobic region, rendering them highly amphiphilic. Class II hydrophobins such as HFBI self-assemble into monolayers at water-air or water-oil interfaces, revealing long-range ordered hexagonal ‘honeycomb’ structures[1]. This property allows for the preparation of pure-protein bilayers and vesicles [2] with unexpectedly low permeability for water and ions. To provide a molecular explanation for these properties, we carried out atomistic and coarse grained molecular dynamics (MD) simulations of HFBI bilayers.
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