Degradation of Fungal Prion HET-s(218-289) Induces Formation of a Generic Amyloid Fold

The prion-forming domain of the fungal prion protein HET-s, HET-s(218-289), is known from solid-state NMR studies to have a β-solenoidal structure; the β-solenoid has the cross-β structure characteristic of all amyloids, but is inherently more complex than the generic stacked β-sheets found in studi...

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Hlavní autoři: Wan, William, Wille, Holger, Stöhr, Jan, Baxa, Ulrich, Prusiner, Stanley B., Stubbs, Gerald
Médium: Artigo
Jazyk:Inglês
Vydáno: The Biophysical Society 2012
Témata:
Protein
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3353098/
https://ncbi.nlm.nih.gov/pubmed/22677387
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2012.04.011
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