Please use this identifier to cite or link to this item: https://apo.ansto.gov.au/dspace/handle/10238/5279
Title: Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity
Authors: Morris, VK
Linser, R
Wilde, KL
Duff, AP
Sunde, M
Kwan, AH
Keywords: Proteins
Spin
Nuclear magnetic resonance
Spectroscopy
Proteins
Identification systems
Issue Date: 1-Jan-2012
Publisher: Wiley-VCH Verlag GMBH
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
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
Gov't Doc #: 4571
URI: http://dx.doi.org/10.1002/anie.201205625
http://apo.ansto.gov.au/dspace/handle/10238/5279
ISSN: 1433-7851
Appears in Collections:Journal Articles

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