Atomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein
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DOI: 10.1038/s41598-019-55661-2
Abstract: Destabilization of prion protein induces a conformational change from normal prion protein (PrPC) to abnormal prion protein (PrPSC). Hydrophobic interaction is the main driving force for protein folding, and critically affects the stability and solvability.… read more here.
Keywords: pathological mutants; hydrophobic core; prion protein;