Solid-state NMR sequential assignments of the amyloid core of Sup35pNM View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2014-10

AUTHORS

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

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. More... »

PAGES

365-370

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12104-013-9518-y

DOI

http://dx.doi.org/10.1007/s12104-013-9518-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016192434

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23934139


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