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Article Dans Une Revue Biomolecular NMR Assignments Année : 2014

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

Résumé

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 β-sheet secondary-structured amino acids that form the fibril core.

Dates et versions

hal-01181118 , version 1 (29-07-2015)

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Citer

Nina Luckgei, Anne K Schütz, Birgit Habenstein, Luc Bousset, Yannick Sourigues, et al.. Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.. Biomolecular NMR Assignments, 2014, 8 (2), pp.365-70. ⟨10.1007/s12104-013-9518-y⟩. ⟨hal-01181118⟩
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