Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: A well-ordered β-sheet core amidst structural heterogeneity.
- Morris, V.
- Linser, R.
- Wilde, K.
- Duff, A.
- Stunde, M.
- Kwan, A.
DOIAbstract
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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