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GrEASy fibrils: Hydrophobins are fungal proteins that assemble into an amphipathic fibrillar monolayer with amyloid properties and a hydrophobic face as water‐resistant as Teflon. Solid‐state NMR studies on EAS hydrophobin fibrils reveal direct evidence of a partial molecular rearrangement on assembly and an ordered β‐sheet‐rich core in the context of a whole protein in this functional amyloid.
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