Antiparallel Arrangement of the Helices of Vesicle-Bound α-Synuclein

Drescher, Malte and Veldhuis, Gertjan and Rooijen van, Bart D. and Milikisyants, Sergey and Subramaniam, Vinod and Huber, Martina (2008) Antiparallel Arrangement of the Helices of Vesicle-Bound α-Synuclein. Journal of the American Chemical Society, 130 (25). pp. 7796-7797. ISSN 0002-7863

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Abstract:	α-Synuclein (αS) is the main component of Lewy bodies from Parkinson’s disease. That αS binds to membranes is known, but the conformation it adopts is still unclear. Pulsed EPR on doubly spin-labeled variants of αS sheds light on the most likely structure. For αS 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 αS on membranes.
Item Type:	Article
Copyright:	© 2008 American Chemical Society
Faculty:	Science and Technology (TNW)
Research Group:	Nano-Biophysics (NBP)
Link to this item:	http://purl.utwente.nl/publications/75522
Official URL:	http://dx.doi.org/10.1021/ja801594s
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Metis ID: 248978