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

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Luckgei, Nina | Schütz, Anne K | Habenstein, Birgit | Bousset, Luc | Sourigues, Yannick | Melki, Ronald | Meier, Beat H | Böckmann, Anja

Edité par CCSD ; Springer -

International audience. 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.

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