期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 130, 期 25, 页码 7796-+出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja801594s
关键词
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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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