Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity
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Date
2012-01-01
Journal Title
Journal ISSN
Volume Title
Publisher
Wiley-VCH Verlag GMBH
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. © 2012, Wiley-VCH Verlag GmbH & Co. KGaA
Description
Keywords
Proteins, Spin, Nuclear magnetic resonance, Spectroscopy, Proteins, Identification systems
Citation
Morris, V. K., Linser, R., Wilde, K. L., Duff, A. P., Sunde, M., & Kwan, A. H. (2012). 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(50), 12621-12625. doi:10.1002/anie.201205625