Ontology highlight
ABSTRACT:
SUBMITTER: De Simone A
PROVIDER: S-EPMC1929054 | biostudies-literature | 2007 Aug
REPOSITORIES: biostudies-literature
Biophysical journal 20070504 4
Misfolding and aggregation of the prion protein (PrP) is responsible for the development of transmissible spongiform encephalopathies (TSE). To gain insights into possible aggregation-prone intermediate states, we construct the free energy surface of the C-terminal globular domain of the PrP from enhanced sampling of replica exchange molecular dynamics. This cellular domain is characterized by three helices H1-H3 and a small beta-sheet. In agreement with experimental studies, the partially unfol ...[more]