Hauptseite > Publikationsdatenbank > Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations > print |
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245 | _ | _ | |a Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations |
260 | _ | _ | |a Cambridge |c 2016 |b RSC Publ. |
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520 | _ | _ | |a 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. |
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700 | 1 | _ | |a Fernandez, C. O. |0 P:(DE-HGF)0 |b 5 |
700 | 1 | _ | |a Carloni, P. |0 P:(DE-Juel1)145614 |b 6 |e Corresponding author |
773 | _ | _ | |a 10.1039/C5CP04549E |g Vol. 18, no. 8, p. 5702 - 5706 |0 PERI:(DE-600)1476244-4 |n 8 |p 5702 - 5706 |t Physical chemistry, chemical physics |v 18 |y 2016 |x 1463-9084 |
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