Abstract
Hydrophobins are small, globular proteins with amphiphilic character that are produced and secreted by filamentous fungi. At hydrophobic-hydrophilic interfaces they self-assemble into durable amyloid-containing structures, called rodlets, which create protective, water repellent coatings for fungal spores. Current models of hydrophobin self-assembly predict that hydrophobin monomers undergo a conformational change at a hydrophobic-hydrophilic interface and integrate into a growing rodlet, however the mechanistic details of rodlet assembly are unknown.
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