Fungal prion proteins studied by solid-state NMR

被引:7
作者
Lange, Adam [1 ]
Meier, Beat [1 ]
机构
[1] ETH, CH-8093 Zurich, Switzerland
关键词
amyloid; prion; HET-s; solid state NMR; magic angle spinning;
D O I
10.1016/j.crci.2007.08.014
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The progress of solid-state NMR obtaining atomic-resolution structural information for amyloid forming proteins is reviewed using the example of fungal prions. A detailed atomic resolution structure of an amyloid fibril is currently still missing. The main focus of this review is on the amyloid-forming fragment 218-289 of the prion protein HET-s of the filamentous fungus Podospora anserina. This prion exhibits the narrowest NMR resonance lines described so far for an amyloid and is therefore a favorable model system for such studies. Potential bottle-necks for three-dimensional structural determination, such as inherent conformational disorder, are discussed and the prospects for improvement in the methodological aspects and in sample preparation are discussed.
引用
收藏
页码:332 / 339
页数:8
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