期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 206, 期 1, 页码 36-42出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2018.04.002
关键词
Prions; Amyloids; Protein aggregation; Paramagnetic solid-state NMR; Hydrogen/deuterium exchange
资金
- National Science Foundation [MCB-1243461, MCB-1715174]
- National Institutes of Health [R01GM094357, S10OD012303, P01A1106705, R01NS083687]
- Camille & Henry Dreyfus Foundation (Camille Dreyfus Teacher-Scholar Award)
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 C-13, N-15-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.
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