Issue 8, 2016

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

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.

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

Supplementary files

Article information

Article type
Communication
Submitted
31 7 2015
Accepted
03 11 2015
First published
04 11 2015

Phys. Chem. Chem. Phys., 2016,18, 5702-5706

Author version available

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

G. Rossetti, F. Musiani, E. Abad, D. Dibenedetto, H. Mouhib, C. O. Fernandez and P. Carloni, Phys. Chem. Chem. Phys., 2016, 18, 5702 DOI: 10.1039/C5CP04549E

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