Direct Evidence of Coexisting Horseshoe and Extended Helix Conformations of Membrane-Bound Alpha-Synuclein

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ChemPhysChem. 2011, 12(2), pp. 267-269. ISSN 1439-4235. eISSN 1439-7641. Available under: doi: 10.1002/cphc.201000815
Zusammenfassung

The physiologically relevant conformation of membrane-bound α-Synuclein (αS) can be either a horseshoe or an extended helix structure. Experimental data obtained by site-directed spin labeling in combination with pulsed electron paramagnetic resonance provide compelling evidence of the coexistence of the horseshoe structure and an extended helix of αS bound to a membrane surface, and potentially resolve the debate on the structure of membrane-bound αS.

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540 Chemie
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electron paramagnetic resonance, membranes, proteins, site-directed spin labeling, vesicles
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ISO 690ROBOTTA, Marta, Patrick BRAUN, Vinod SUBRAMANIAM, Martina HUBER, Malte DRESCHER, Bart D. van ROOIJEN, 2011. Direct Evidence of Coexisting Horseshoe and Extended Helix Conformations of Membrane-Bound Alpha-Synuclein. In: ChemPhysChem. 2011, 12(2), pp. 267-269. ISSN 1439-4235. eISSN 1439-7641. Available under: doi: 10.1002/cphc.201000815
BibTex
@article{Robotta2011-02-07Direc-16109,
  year={2011},
  doi={10.1002/cphc.201000815},
  title={Direct Evidence of Coexisting Horseshoe and Extended Helix Conformations of Membrane-Bound Alpha-Synuclein},
  number={2},
  volume={12},
  issn={1439-4235},
  journal={ChemPhysChem},
  pages={267--269},
  author={Robotta, Marta and Braun, Patrick and Subramaniam, Vinod and Huber, Martina and Drescher, Malte and Rooijen, Bart D. van}
}
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