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

G. Rossetti; F. Musiani; E. Abad; D. Dibenedetto; H. Mouhib; C. O. Fernandez; P. Carloni

doi:10.1039/c5cp04549e

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

G. Rossetti, F. Musiani, E. Abad, D. Dibenedetto, H. Mouhib, C. O. Fernandez, P. Carloni^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

We perform here enhanced sampling simulations of N-terminally acetylated human ?-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 ?-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.

Original language	English
Pages (from-to)	5702-5706
Journal	Physical Chemistry Chemical Physics
Volume	18
Issue number	8
DOIs	https://doi.org/10.1039/c5cp04549e
Publication status	Published - 28 Feb 2016

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Cite this

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title = "Conformational ensemble of human alpha-synuclein physiological form predicted by molecular simulations",

abstract = "We perform here enhanced sampling simulations of N-terminally acetylated human ?-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 ?-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.",

author = "G. Rossetti and F. Musiani and E. Abad and D. Dibenedetto and H. Mouhib and Fernandez, {C. O.} and P. Carloni",

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AU - Rossetti, G.

AU - Musiani, F.

AU - Abad, E.

AU - Dibenedetto, D.

AU - Mouhib, H.

AU - Fernandez, C. O.

AU - Carloni, P.

PY - 2016/2/28

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AB - We perform here enhanced sampling simulations of N-terminally acetylated human ?-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 ?-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.

U2 - 10.1039/c5cp04549e

DO - 10.1039/c5cp04549e

M3 - Article

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VL - 18

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EP - 5706

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JF - Physical Chemistry Chemical Physics

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