Fungal prion proteins studied by solid-state NMR

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.