ausblenden:
Schlagwörter:
amyloids; fibrous proteins; hydrophobins; magic-angle spinning; solid-state NMR spectroscopy
Zusammenfassung:
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.
