Article
Use of molecular dynamics simulation to explore structural facets of human prion protein with pathogenic mutations.
Biophysical chemistry - 1 Jun 2016
Borgohain Gargi, Dan Nirnoy, Paul Sandip
Abstract excerpt
Prion diseases are caused by mutations at different positions of the prion protein. A large number of pathogenic mutations are reported in the literature. Two of such point mutations T193I and R148H located at two different helical strands (H2 and H1) of the prion protein associated with fCJD (familial Creutzfeld-Jacob disease) are studied. We have used classical molecular dynamics (MD) simulation technique to...
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