Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR

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

C-terminal prion forming domain, UNP residues 218-289

Solid-State NMR; The structure of seven HET-s(218-289) prion molecules in their amyloid conformation has been calculated. The 20 lowest energy structures of the five central molecules are provided here, to avoid artefactual border effects.

the study has been performed by solid-state NMR.

The structure of seven HET-s(218-289) prion molecules in their amyloid conformation has been calculated. The 20 lowest energy structures of the five central molecules are provided here, to avoid artefactual border effects.

HET-s(218-289), beta-solenoid, prion, amyloid fibril, parallel beta-sheets, hydrophobic core, salt bridges, asparagine ladders, beta-helix, PROTEIN FIBRIL