Communication
High-Resolution Solid-State NMR Spectroscopy of the Prion Protein HET-s in Its Amyloid Conformation†
†
We are grateful to Andreas Hunkeler and Urban Meier for their technical support, to Dr. René Verel and Rochus Keller for scientific advice, and to Dr. Thorsten Luehrs for the EM pictures. This work was supported by the Swiss National Science Foundation (SNF) and the ETH Zurich.
Graphical 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.
