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

G. Rossetti, F. Musiani, E. Abad, D. Dibenedetto, H. Mouhib, C. O. Fernandez, P. Carloni*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review


We perform here enhanced sampling simulations of N-terminally acetylated human ?-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 ?-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.
Original languageEnglish
Pages (from-to)5702-5706
JournalPhysical Chemistry Chemical Physics
Issue number8
Publication statusPublished - 28 Feb 2016

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