Jump to main content
Jump to site search

Issue 8, 2016
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 31 Jul 2015, accepted on 03 Nov 2015 and first published on 04 Nov 2015


Article type: Communication
DOI: 10.1039/C5CP04549E
Author version
available:
Download author version (PDF)
Phys. Chem. Chem. Phys., 2016,18, 5702-5706

  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements