ArticleBiochemistry2014
Fiber diffraction of the prion-forming domain HET-s(218-289) shows dehydration-induced deformation of a complex amyloid structure.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Femtosecond X-ray coherent diffraction of aligned amyloid fibrils on low background graphene.Nature communications · 2018Article
- Structural Biology of PrP Prions.Cold Spring Harbor perspectives in medicine · 2017Review
- The HET-S/s Prion Motif in the Control of Programmed Cell Death.Cold Spring Harbor perspectives in biology · 2016Review
- Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.Nature structural & molecular biology · 2016Article
- NMR WaterLOGSY Reveals Weak Binding of Bisphenol A with Amyloid Fibers of a Conserved 11 Residue Peptide from Androgen Receptor.PloS one · 2016Article
- Structural studies of truncated forms of the prion protein PrP.Biophysical journal · 2015Article
- Truncated forms of the prion protein PrP demonstrate the need for complexity in prion structure.Prion · 2015Article
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2 authors.
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Abstract
Amyloids are filamentous protein aggregates that can be formed by many different proteins and are associated with both disease and biological functions. The pathogenicities or biological functions of amyloids are determined by their particular molecular structures, making accurate structural models a requirement for understanding their biological effects. One potential factor that can affect amyloid structures is hydration. Previous studies of simple stacked β-sheet amyloids have suggested that dehydration does not impact structure, but other studies indicated dehydration-related structural changes of a putative water-filled nanotube. Our results show that dehydration significantly affects the molecular structure of the fungal prion-forming domain HET-s(218-289), which forms a β-solenoid with no internal solvent-accessible regions. The dehydration-related structural deformation of HET-s(218-289) indicates that water can play a significant role in complex amyloid structures, even when no obvious water-accessible cavities are present.
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