%0 Journal Article
%A Rossetti, Giulia
%A Musiani, F.
%A Abad, E.
%A Dibenedetto, D.
%A Mouhib, H.
%A Fernandez, C. O.
%A Carloni, P.
%T Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
%J Physical chemistry, chemical physics
%V 18
%N 8
%@ 1463-9084
%C Cambridge
%I RSC Publ.
%M FZJ-2016-05813
%P 5702 - 5706
%D 2016
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000371953000003
%$ pmid:26553504
%R 10.1039/C5CP04549E
%U https://juser.fz-juelich.de/record/820521