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Biomol NMR Assign. 2017 Apr;11(1):75-80. doi: 10.1007/s12104-016-9723-6. Epub 2016 Dec 21.

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

Author information

1
Department of Chemistry and Biochemistry, The Ohio State University, 222 CBEC Building, 151 West Woodruff Avenue, Columbus, OH, 43210, USA.
2
Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106, USA.
3
Department of Chemistry and Biochemistry, The Ohio State University, 222 CBEC Building, 151 West Woodruff Avenue, Columbus, OH, 43210, USA. jaroniec.1@osu.edu.

Abstract

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.

KEYWORDS:

Amyloid; Magic-angle spinning; Prion protein; Solid-state NMR

PMID:
28004358
PMCID:
PMC5344711
DOI:
10.1007/s12104-016-9723-6
[Indexed for MEDLINE]
Free PMC Article

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