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

Autor: Rossetti, G., Musiani, F., Abad, E., Dibenedetto, D., Mouhib, H., Fernandez, C. O., Carloni, P.
Zdroj: Physical Chemistry Chemical Physics (PCCP); 2/28/2016, Vol. 18 Issue 8, p5702-5706, 5p
Abstrakt: 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. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index