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Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy
- Source :
- Journal of Structural Biology. 206:36-42
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
Abstract
- The C-terminally truncated Y145Stop variant of prion protein (PrP23-144), which is associated with heritable PrP cerebral amyloid angiopathy in humans and also capable of triggering a transmissible prion disease in mice, serves as a useful in vitro model for investigating the molecular and structural basis of amyloid strains and cross-seeding specificities. Here, we determine the protein-solvent interfaces in human PrP23-144 amyloid fibrils generated from recombinant (13)C,(15)N-enriched protein and incubated in aqueous solution containing paramagnetic Cu(II)-EDTA, by measuring residue-specific (15)N longitudinal paramagnetic relaxation enhancements using two-dimensional magic-angle spinning solid-state NMR spectroscopy. To further probe the interactions of the amyloid core residues with solvent molecules we perform complementary measurements of amide hydrogen/deuterium exchange detected by solid-state NMR and solution NMR methods. The solvent accessibility data are evaluated in the context of the structural model for human PrP23-144 amyloid.
- Subjects :
- Microscopy, Electron, Scanning Transmission
Amyloid
Magnetic Resonance Spectroscopy
Prions
Amyloidogenic Proteins
Context (language use)
Article
Prion Proteins
Mice
03 medical and health sciences
Structural Biology
medicine
Animals
Humans
Molecule
030304 developmental biology
Carbon Isotopes
0303 health sciences
Aqueous solution
Nitrogen Isotopes
Chemistry
030302 biochemistry & molecular biology
Deuterium Exchange Measurement
Nuclear magnetic resonance spectroscopy
medicine.disease
Solutions
Solid-state nuclear magnetic resonance
Codon, Nonsense
Solvents
Biophysics
Hydrogen–deuterium exchange
Cerebral amyloid angiopathy
Subjects
Details
- ISSN :
- 10478477
- Volume :
- 206
- Database :
- OpenAIRE
- Journal :
- Journal of Structural Biology
- Accession number :
- edsair.doi.dedup.....36d2b893901bbb4e140727e799074c33