Probing the early stages of prion protein (PrP) aggregation with atomistic molecular dynamics simulations
Chemical Communications2018Vol. 54(57), pp. 8007–8010
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Abstract
Prions are self-replicating infectious proteinaceous agents whose conformations are capable of forming amyloid-like aggregate fibrils. Here we present molecular dynamics simulations aimed at investigating the aggregation process of the β-rich H2H3 domain of the ovine prion protein (H2H3-OvPrPSc), known to be the portion of prion protein carrying oligomerization activity.
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