Publikation:

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

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Datum

2011

Autor:innen

Huber, Martina
Rooijen, Bart D. van

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http://nbn-resolving.de/urn:nbn:de:bsz:352-161090
DOI (zitierfähiger Link)
https://doi.org/10.1002/cphc.201000815
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Open Access-Veröffentlichung
Open Access Green

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Chemie: Publikationen
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Published

Erschienen in

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.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
540 Chemie

Schlagwörter

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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