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

Morris, V. K., Linser, R., Wilde, K. L., Duff, A. P., Stunde, 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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-A67D-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C523-0
Genre: Journal Article

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1977600.pdf (Publisher version), 2MB
 
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 Creators:
Morris, V. K., Author
Linser, R.1, Author              
Wilde, K. L., Author
Duff, A. P., Author
Stunde, M., Author
Kwan, A. H., Author
Affiliations:
1Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society, ou_1950286              

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Free keywords: amyloids; fibrous proteins; hydrophobins; magic-angle spinning; solid-state NMR spectroscopy
 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.

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Language(s): eng - English
 Dates: 2012-11-042012-12-07
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201205625
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Title: Angewandte Chemie International Edition
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Source Genre: Journal
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Pages: - Volume / Issue: 51 (50) Sequence Number: - Start / End Page: 12621 - 12625 Identifier: -