Chembiochem : a European journal of chemical biology
A combined solid-state NMR and MD characterization of the stability and dynamics of the HET-s(218-289) prion in its amyloid conformation.

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core.

13C, 15N resonance assignment of parts of the HET-s prion protein in its amyloid form.

HET-s(218-289): C-terminal prion forming domain of the HET-s protein.
The sequence of the molecule is numbered from 217 to 296. The residues 218-289 correspond to HET-s(218-289).

High-Resolution Structure Of The Het-S(218-289) Prion In Its Amyloid Form Obtained By Solid-State Nmr

Haddock Calculated Model Of Congo Red Bound To The Het-S Amyloid

Structure Of The Het-s(218-289) Prion In Its Amyloid Form Obtained By Solid-state Nmr

s gene 30 kDa polypeptide [Podospora anserina=fungus, Peptide, 289 aa]

RecName: Full=Heterokaryon incompatibility protein s; AltName: Full=Small s protein; AltName: Full=Vegetative incompatibility p

Solid-state NMR assignment of the rigid core of the HET-s(218-289) prion protein in its amyloid conformation.

All experiments were recorded with a rotation at the magic angle.

Solid-state NMR assignment of the HET-s(218-289) amyloid fibrils.

Structure of the HET-s(218-289) amyloid fibrils.

"Wet" fibrils sample: the total amount of water in the sample is at least 60% (weight). Below, the concentration is given with respect to the total protein concentration.

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax