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 |
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| container_issue | 48 |
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| container_title | Angewandte Chemie International Edition |
| container_volume | 52 |
| creator | Luckgei, Nina Schütz, Anne K. Bousset, Luc Habenstein, Birgit Sourigues, Yannick Gardiennet, Carole Meier, Beat H. Melki, Ronald Böckmann, Anja |
| description | 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. |
| doi_str_mv | 10.1002/anie.201304699 |
| format | Article |
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| language | eng |
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| source | Wiley Online Library - AutoHoldings Journals |
| subjects | fibrils prions proteins solid-state NMR spectroscopy Sup35p |
| title | The Conformation of the Prion Domain of Sup35 p in Isolation and in the Full-Length Protein |
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