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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Format: | Artikel |
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. |
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ISSN: | 1433-7851 1521-3773 |
DOI: | 10.1002/anie.201304699 |