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

Abstract

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. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.