Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity

Vanessa K Morris; Rasmus Linser; Karyn L Wilde; Anthony P Duff; Margaret Sunde; Ann H Kwan

doi:10.1002/anie.201205625

Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity

Angew Chem Int Ed Engl. 2012 Dec 7;51(50):12621-5. doi: 10.1002/anie.201205625. Epub 2012 Nov 4.

Authors

Vanessa K Morris¹, Rasmus Linser, Karyn L Wilde, Anthony P Duff, Margaret Sunde, Ann H Kwan

Affiliation

¹ School of Medical Sciences and School of Molecular Bioscience, University of Sydney, Sydney, Australia.

PMID: 23125123
DOI: 10.1002/anie.201205625

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.

MeSH terms

Amino Acid Sequence
Amyloid / chemistry*
Circular Dichroism
Fungal Proteins / chemistry*
Fungi / metabolism
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Protein Structure, Secondary

Substances

Amyloid
Fungal Proteins