Partially-Deuterated Samples of HET-s(218-289) Fibrils: Assignment and Deuterium Isotope Effect

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

Journal of the American Chemical Society
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.

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).

HET-s backbone assignments and deuterium isotope effect investigation

rigid core of the HET-s(218-289) prion protein in its amyloid conformation

Uniformly 13C, 15N, 2H labelled HET-s (218-289), fibrillized
in H2O for 100% back exchange of 1H at exchangeable sites.

Uniformly 13C,15N HET-s(218-289) grown in uniformly 2H,13C labelled glucose and
25%/75% D2O/H2O for 25% protonation at the HA positions, and reduced protation
elsewhere. Fibrillized in 100% D2O for no protonation at exchangeable sites.

Uniformly 13C,15N HET-s(218-289) grown in uniformly 2H,13C labelled glucose and
25%/75% D2O/H2O for 25% protonation at the HA positions, and reduced protation
elsewhere. Fibrillized in 100% H2O for full protonation at exchangeable sites.