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 …

A molecular understanding of the prion diseases requires delineation of the origin of
misfolding of the prion protein (PrP). An understanding of how different disease‐linked …

We compare the folding equilibrium of the globular domain of the human prion protein with
two variants of this domain, for which an additional disulfide bond was introduced into the …

We study the thermodynamic stability of the native state of the human prion protein using a
new free-energy method, replica-exchange on-the-fly parameterization. This method is …

The existence of several prion strains and their capacity of overcoming species barriers
seem to point to a high conformational adaptability of the prion protein. To investigate this …

The post-translational conversion of the ubiquitously expressed cellular form of the prion
protein, PrPC, into its misfolded and pathogenic isoform, known as prion or PrPSc, plays a …

The structural transition of the prion protein from α-helical-to β-sheet-rich underlies its
conversion into infectious and disease-associated isoforms. Here we describe the crystal …

Molecular dynamics simulation method is used to assess the contribution of a disease-
associated salt bridge in the early stages of the conformational rearrangement of human …

To gain insight into the structural mechanism of the conformational conversion process of
prion, we examined the potential amyloidogenic property of each secondary structural …

Prion diseases are fatal transmissible neurodegenerative diseases that result from structural
conversion of the prion protein into a disease-associated isoform. The prion protein contains …