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

Vanessa K Morris1, Rasmus Linser, Karyn L Wilde

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

Angewandte Chemie (International Ed. in English)
|November 6, 2012
PubMed

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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