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Vanessa K. Morris, Rasmus Linser, Karyn L. Wilde, Anthony P. Duff, Margaret Sunde and Ann H. Kwan Solid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural Heterogeneity Angewandte Chemie International Edition 51

Article first published online: 4 NOV 2012 | DOI: 10.1002/anie.201205625

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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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