Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations. Issue 8 (10th November 2015)

• Record Type: Journal Article
• Authors: Rossetti, G.; Musiani, F.; Abad, E.; Dibenedetto, D.; Mouhib, H.; Fernandez, C. O.; Carloni, P.
• Is Part Of: Physical chemistry chemical physics. Volume 18:Issue 8(2016)
• Page Start: 5702
• Page End: 5706
• Publication Date: 2015-11-10
• Subjects: Chemistry, Physical and theoretical -- Periodicals; 541.3
• DOI: 10.1039/c5cp04549e
• Languages: English
• ISSNs: 1463-9076

Abstract

Abstract : Enhanced sampling simulations of N-terminally acetylated human α-synuclein suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix altering protein dynamics at the N-terminal and intramolecular interactions. 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.