We perform here enhanced sampling simulations of N-terminally acetylated human α-synuclein, an intrinsically disordered protein involved in Parkinson's disease. The calculations, consistent with experiments, suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.

Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations

MUSIANI, FRANCESCO;
2016

Abstract

We perform here enhanced sampling simulations of N-terminally acetylated human α-synuclein, an intrinsically disordered protein involved in Parkinson's disease. The calculations, consistent with experiments, suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.
Rossetti, G.; Musiani, F.; Abad, E.; Dibenedetto, D.; Mouhib, H.; Fernandez, C.O.; Carloni, P.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/585372
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