Contribution of Specific Residues of the β-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability
Figure 4
2D Solid state NMR spectra of Ala variants of HET-s(218–289) amyloid fibrils.
The 2D DARR solid state NMR spectra of 15N,13C-labeled Ala variants of HET-S(218–289) amyloid fibrils are shown on top of the corresponding spectrum of wild-type HET-s(218–289) amyloid fibrils, the latter which contour lines are color-coded black. The spectra are labelled according to the amino acid replacement. The close resemblance between the variant and the wild-type spectra indicates the conservation of the β-solenoid fold in the variants with the exception for G278A and the double variant F286A/W287A. In Figure S3 the same spectra are shown including the assignment of wild-type HET-s(218–289) amyloid fibrils [29].