The Conformation of the Prion Domain of Sup35 p in Isolation and in the Full-Length Protein

The whole is not the sum of the parts: Fibrils form both from the full‐length Sup35 prion protein and also from its isolated NM domain. A conformation analysis of both shows that Sup35NM and fragments thereof, which are often used as convenient models for prion fibril assembly, have a very different...

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Veröffentlicht in:Angewandte Chemie International Edition 2013-11, Vol.52 (48), p.12741-12744
Hauptverfasser: Luckgei, Nina, Schütz, Anne K., Bousset, Luc, Habenstein, Birgit, Sourigues, Yannick, Gardiennet, Carole, Meier, Beat H., Melki, Ronald, Böckmann, Anja
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Sprache:eng
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Zusammenfassung:The whole is not the sum of the parts: Fibrils form both from the full‐length Sup35 prion protein and also from its isolated NM domain. A conformation analysis of both shows that Sup35NM and fragments thereof, which are often used as convenient models for prion fibril assembly, have a very different conformation of the prion domains.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201304699