13C and 15N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils
| Autor: | Krystyna Surewicz, Philippe S. Nadaud, Theint Theint, Witold K. Surewicz, Christopher P. Jaroniec |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Amyloid Chemistry Hamster 010402 general chemistry Amyloid fibril 01 natural sciences Biochemistry Article 0104 chemical sciences In vitro model 03 medical and health sciences 030104 developmental biology Solid-state nuclear magnetic resonance Structural Biology Magic angle spinning Prion protein Peptide sequence |
| Zdroj: | Biomolecular NMR Assignments. 11:75-80 |
| ISSN: | 1874-270X 1874-2718 |
| DOI: | 10.1007/s12104-016-9723-6 |
| Popis: | 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 13C and 15N 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. |
| Databáze: | OpenAIRE |
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