Using high-resolution NMR spectroscopy, the Schwalbe group could characterize the
unfolded state of the human prion protein in its SS-oxidized and-reduced state. NMR
analysis shows that the unfolded state has three stretches of residual beta-sheet character.
In addition, several hydrophobic clusters can be identified. Most strikingly, the introduction of
the native disulfide bridge considerably rigidifies the entire protein. This phenomenon is
linked to fibril formation properties of the prion protein. The polypeptide chain forms fibrils …