The Conformation of the Prion Domain of Sup35 p in Isolation and in the Full‐Length Protein1. Issue 48 (9th October 2013)

• Record Type: Journal Article
• Authors: Luckgei, Nina; Schütz, Anne K.; Bousset, Luc; Habenstein, Birgit; Sourigues, Yannick; Gardiennet, Carole; Meier, Beat H.; Melki, Ronald; Böckmann, Anja
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 48(2013)
• Page Start: 12741
• Page End: 12744
• Publication Date: 2013-10-09
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201304699
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The whole is not the sum of the parts</bold>: 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.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg4t7btx4m" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>