Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.
 

Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.

Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.

Biomol NMR Assign. 2013 Aug 10;

Authors: Luckgei N, Schütz AK, Habenstein B, Bousset L, Sourigues Y, Melki R, Meier BH, Böckmann A

Abstract
Sup35pNM represents the N-terminal and middle (M) domains of the yeast Saccharomyces cerevisiae prion Sup35p. This fragment is commonly used for structural and functional studies of Sup35p. We here present a solid-state NMR study of fibrils formed by this fragment and show that sequential assignments can be obtained for the rigid and well-ordered parts of the protein using 3D spectroscopy. We describe in detail the sequential assignment of the 22 residues yielding strong, narrow signals with chemical shifts that correspond mostly to ?-sheet secondary-structured amino acids that form the fibril core.


PMID: 23934139 [PubMed - as supplied by publisher]



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