Publikation: Antiparallel Arrangement of the Helices of Vesicle-Bound α-Synuclein
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2008
Autor:innen
Veldhuis, Gertjan
Rooijen, Bart D. van
Milikisyants, Sergey
Huber, Martina
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Journal of the American Chemical Society. 2008, 130(25), pp. 7796-7797. ISSN 0002-7863. eISSN 1520-5126. Available under: doi: 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.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
540 Chemie
Schlagwörter
dodecyl-sulfate micelles, parkinsons-disease, spectroscopy, dynamics, binding, protein, EPR, association, membranes, variants
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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 α-Synuclein. In: Journal of the American Chemical Society. 2008, 130(25), pp. 7796-7797. ISSN 0002-7863. eISSN 1520-5126. Available under: doi: 10.1021/ja801594sBibTex
@article{Drescher2008Antip-1110,
year={2008},
doi={10.1021/ja801594s},
title={Antiparallel Arrangement of the Helices of Vesicle-Bound α-Synuclein},
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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