Biomolecular NMR Assignments

, Volume 11, Issue 1, pp 75–80 | Cite as

13C and 15N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils

  • Theint Theint
  • Philippe S. Nadaud
  • Krystyna Surewicz
  • Witold K. Surewicz
  • Christopher P. JaroniecEmail author


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.


Prion protein Amyloid Magic-angle spinning Solid-state NMR 



This research was supported by NIH (Grants R01GM094357 and S10OD012303 to C.P.J. and P01AI106705 and R01NS083687 to W.K.S.) and the Camille & Henry Dreyfus Foundation (Camille Dreyfus Teacher-Scholar Award to C.P.J.).


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Copyright information

© Springer Science+Business Media Dordrecht 2016

Authors and Affiliations

  1. 1.Department of Chemistry and BiochemistryThe Ohio State UniversityColumbusUSA
  2. 2.Department of Physiology and BiophysicsCase Western Reserve UniversityClevelandUSA

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