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  • Title: Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity.
    Author: Morris VK, Linser R, Wilde KL, Duff AP, Sunde M, Kwan AH.
    Journal: Angew Chem Int Ed Engl; 2012 Dec 07; 51(50):12621-5. PubMed ID: 23125123.
    Abstract:
    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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