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• W2808465223 abstract "Abstract Hydrophobins are fungal proteins that can self-assemble into amphiphilic films at hydrophobic-hydrophilic interfaces. Class I hydrophobin aggregates resemble amyloid fibrils, sharing some features with them. Here, five site-directed mutants of Vmh2, a member of basidiomycota class I hydrophobins, were designed and characterized to elucidate the molecular determinants playing a key role in class I hydrophobin self-assembly. The mechanism of fibril formation proposed for Vmh2 foresees that the triggering event is the destabilization of a specific loop (L1), leading to the formation of a β-hairpin, which in turn generates the β-spine of the amyloid fibril." @default.
• W2808465223 created "2018-06-21" @default.
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• W2808465223 date "2018-06-20" @default.
• W2808465223 modified "2023-10-16" @default.
• W2808465223 title "New clues into the self-assembly of Vmh2, a basidiomycota class I hydrophobin" @default.
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• W2808465223 doi "https://doi.org/10.1515/hsz-2018-0124" @default.
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