title: Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity.
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.
authors.affiliation: School of Medical Sciences and School of Molecular Bioscience, University of Sydney, Sydney, Australia.
authors.forename: Vanessa K
authors.initials: VK
authors.lastname: Morris
authors.forename: Rasmus
authors.initials: R
authors.lastname: Linser
authors.forename: Karyn L
authors.initials: KL
authors.lastname: Wilde
authors.forename: Anthony P
authors.initials: AP
authors.lastname: Duff
authors.forename: Margaret
authors.initials: M
authors.lastname: Sunde
authors.forename: Ann H
authors.initials: AH
authors.lastname: Kwan
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D002942:Circular Dichroism; D005656:Fungal Proteins / Q000737:chemistry*; D005658:Fungi / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary
chemical_list: D000682:Amyloid; D005656:Fungal Proteins