The Conformation of the Prion Domain of Sup35p in Isolation and in the Full-Length Protein

被引：35

作者：

Luckgei, Nina ^{[1
]}

Schuetz, Anne K. ^{[2
]}

Bousset, Luc ^{[3
]}

Habenstein, Birgit ^{[1
]}

Sourigues, Yannick ^{[3
]}

Gardiennet, Carole ^{[1
]}

Meier, Beat H. ^{[2
]}

Melki, Ronald ^{[3
]}

Boeckmann, Anja ^{[1
]}

机构：

[1] Univ Lyon 1, CNRS, Inst Biol & Chim Prot, UMR 5086, F-69367 Lyon, France

[2] ETH, CH-8093 Zurich, Switzerland

[3] CNRS, Lab Enzymol & Biochim Struct, UPR 3082, F-91198 Gif Sur Yvette, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2013年 / 52卷 / 48期

关键词：

fibrils; prions; proteins; solid-state NMR spectroscopy; Sup35p; SACCHAROMYCES-CEREVISIAE; AMYLOID FIBRILS; SECONDARY STRUCTURE; FUNCTIONAL-ANALYSIS; NMR-SPECTROSCOPY; CHEMICAL-SHIFT; YEAST; TRANSLATION; TERMINATION; VARIANTS;

D O I：

10.1002/anie.201304699

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：12741 / 12744

页数：4

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