Antiparallel Arrangement of the Helices of Vesicle-Bound alpha-Synuclein
| Publikationstyp: | Zeitschriftenartikel |
| Autor/innen: | Drescher, Malte; Veldhuis, Gertjan; Rooijen, Bart D. van; Milikisyants, Sergey; Subramaniam, Vinod; Huber, Martina |
| Erscheinungsjahr: | 2008 |
| Erschienen in: | Journal of the American Chemical Society ; 130 (2008), 25. - S. 7796-7797. - ISSN 0002-7863. - eISSN 1520-5126 |
| Pubmed ID: | 18512917 |
| DOI (zitierfähiger Link): | https://dx.doi.org/10.1021/ja801594s |
| Zusammenfassung: |
alpha-Synuclein (alpha S) is the main component of Lewy bodies from Parkinson's disease. That alpha S binds to membranes is known, but the conformation it adopts is still unclear. Pulsed EPR on doubly spin-labeled variants of alpha S sheds light on the most likely structure. For alpha S bound to vesicles large enough to accommodate also the extended conformation, an antiparallel helix conformation is found. This suggests that the bent structure shown is the preferred conformation of alpha S on membranes.
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| Fachgebiet (DDC): | 540 Chemie |
| Schlagwörter: | dodecyl-sulfate micelles, parkinsons-disease, spectroscopy, dynamics, binding, protein, EPR, association, membranes, variants |
| Universitätsbibliographie: | Ja |
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DRESCHER, Malte, Gertjan VELDHUIS, Bart D. van ROOIJEN, Sergey MILIKISYANTS, Vinod SUBRAMANIAM, Martina HUBER, 2008. Antiparallel Arrangement of the Helices of Vesicle-Bound alpha-Synuclein. In: Journal of the American Chemical Society. 130(25), pp. 7796-7797. ISSN 0002-7863. eISSN 1520-5126. Available under: doi: 10.1021/ja801594s
@article{Drescher2008Antip-1110, title={Antiparallel Arrangement of the Helices of Vesicle-Bound alpha-Synuclein}, year={2008}, doi={10.1021/ja801594s}, number={25}, volume={130}, issn={0002-7863}, journal={Journal of the American Chemical Society}, pages={7796--7797}, author={Drescher, Malte and Veldhuis, Gertjan and Rooijen, Bart D. van and Milikisyants, Sergey and Subramaniam, Vinod and Huber, Martina} }
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