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Updated: May 8, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
Solid-state NMR sequential assignments of the amyloid core of Sup35pNM
Nina Luckgei1, Anne K Schütz, Birgit Habenstein
1Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon, 1, 7 passage du Vercors, 69367, Lyon, France.
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 β-sheet secondary-structured amino acids that form the fibril core.
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