Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 11, Issue 1, Pages 75-80Publisher
SPRINGER
DOI: 10.1007/s12104-016-9723-6
Keywords
Prion protein; Amyloid; Magic-angle spinning; Solid-state NMR
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Funding
- NIH [R01GM094357, S10OD012303, P01AI106705, R01NS083687]
- Camille & Henry Dreyfus Foundation
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The Y145Stop prion protein (PrP23-144), which has been linked to the development of a heritable prionopathy in humans, is a valuable in vitro model for elucidating the structural and molecular basis of amyloid seeding specificities. Here we report the sequential backbone and side-chain C-13 and N-15 assignments of mouse and Syrian hamster PrP23-144 amyloid fibrils determined by using 2D and 3D magic-angle spinning solid-state NMR. The assigned chemical shifts were used to predict the secondary structures for the core regions of the mouse and Syrian hamster PrP23-144 amyloids, and the results compared to those for human PrP23-144 amyloid, which has previously been analyzed by solid-state NMR techniques.
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