Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity
dc.contributor.author | Morris, VK | en_AU |
dc.contributor.author | Linser, R | en_AU |
dc.contributor.author | Wilde, KL | en_AU |
dc.contributor.author | Duff, AP | en_AU |
dc.contributor.author | Sunde, M | en_AU |
dc.contributor.author | Kwan, AH | en_AU |
dc.date.accessioned | 2014-03-24T00:42:01Z | en_AU |
dc.date.available | 2014-03-24T00:42:01Z | en_AU |
dc.date.issued | 2012-01-01 | en_AU |
dc.date.statistics | 2014-03-24 | en_AU |
dc.description.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 | en_AU |
dc.identifier.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 | en_AU |
dc.identifier.govdoc | 4571 | en_AU |
dc.identifier.issn | 1433-7851 | en_AU |
dc.identifier.issue | 50 | en_AU |
dc.identifier.journaltitle | Angewandte Chemie International Edition | en_AU |
dc.identifier.pagination | 12621-12625 | en_AU |
dc.identifier.uri | http://dx.doi.org/10.1002/anie.201205625 | en_AU |
dc.identifier.uri | http://apo.ansto.gov.au/dspace/handle/10238/5279 | en_AU |
dc.identifier.volume | 51 | en_AU |
dc.language.iso | en | en_AU |
dc.publisher | Wiley-VCH Verlag GMBH | en_AU |
dc.subject | Proteins | en_AU |
dc.subject | Spin | en_AU |
dc.subject | Nuclear magnetic resonance | en_AU |
dc.subject | Spectroscopy | en_AU |
dc.subject | Proteins | en_AU |
dc.subject | Identification systems | en_AU |
dc.title | Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity | en_AU |
dc.type | Journal Article | en_AU |
Files
License bundle
1 - 1 of 1
Loading...
- Name:
- license.txt
- Size:
- 1.71 KB
- Format:
- Item-specific license agreed upon to submission
- Description: