High‐Resolution Solid‐State NMR Spectroscopy of the Prion Protein HET‐s in Its Amyloid Conformation

Abstract

Partly present, partly absent: The solid-state NMR spectra (figure, right side) of the amyloid form of the HET-s prion protein (EM image at left) show the resonances for 43 residues with high resolution, whereas 29 residues give no observable NMR signals. A possible explanation could be that the protein structure consists of both highly ordered and strongly disordered domains.