Publikation:

Locally resolved membrane binding affinity of the N-Terminus of α-Synuclein

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2012

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Zijlstra, Niels
Huber, Martina

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http://nbn-resolving.de/urn:nbn:de:bsz:352-198741
DOI (zitierfähiger Link)
https://doi.org/10.1021/bi300357a
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Biologie: Publikationen
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Published

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Biochemistry. 2012, 51(19), pp. 3960-3962. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi300357a

Zusammenfassung

α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson’s disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein−membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform.

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570 Biowissenschaften, Biologie

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ISO 690ROBOTTA, Marta, Christian HINTZE, Stefan SCHILDKNECHT, Niels ZIJLSTRA, Christian JÜNGST, Christiaan KARREMAN, Martina HUBER, Marcel LEIST, Vinod SUBRAMANIAM, Malte DRESCHER, 2012. Locally resolved membrane binding affinity of the N-Terminus of α-Synuclein. In: Biochemistry. 2012, 51(19), pp. 3960-3962. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi300357a
BibTex
@article{Robotta2012-05-15Local-19874,
  year={2012},
  doi={10.1021/bi300357a},
  title={Locally resolved membrane binding affinity of the N-Terminus of α-Synuclein},
  number={19},
  volume={51},
  issn={0006-2960},
  journal={Biochemistry},
  pages={3960--3962},
  author={Robotta, Marta and Hintze, Christian and Schildknecht, Stefan and Zijlstra, Niels and Jüngst, Christian and Karreman, Christiaan and Huber, Martina and Leist, Marcel and Subramaniam, Vinod and Drescher, Malte}
}
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