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Membrane bound α‐synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain

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2013

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Wietek, Jonas
Haralampiev, Ivan
Amoussouvi, Aouefa
Herrmann, Andreas

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https://doi.org/10.1016/j.febslet.2013.06.034
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FEBS Letters. 2013, 587(16), pp. 2572-2577. ISSN 0014-5793. eISSN 1873-3468. Available under: doi: 10.1016/j.febslet.2013.06.034

Zusammenfassung

Cellular pathways involving α‐synuclein (αS) seem to be causative for development of Parkinson's disease. Interactions between αS and lipid membranes appear to be important for the physiological function of the protein and influence the pathological aggregation of αS leading to the formation of amyloid plaques. Upon membrane binding the unstructured αS folds into amphipathic helices. In our work we characterized the penetration depth and probed the local environment of Trp‐residues introduced along the αS sequence. We could show that while the entire helix is well embedded in the lipid bilayer, segments with a shallower penetration and supposable higher flexibility exist.

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570 Biowissenschaften, Biologie

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ISO 690WIETEK, Jonas, Ivan HARALAMPIEV, Aouefa AMOUSSOUVI, Andreas HERRMANN, Martin T. STÖCKL, 2013. Membrane bound α‐synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain. In: FEBS Letters. 2013, 587(16), pp. 2572-2577. ISSN 0014-5793. eISSN 1873-3468. Available under: doi: 10.1016/j.febslet.2013.06.034
BibTex
@article{Wietek2013-08-19Membr-42149,
  year={2013},
  doi={10.1016/j.febslet.2013.06.034},
  title={Membrane bound α‐synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain},
  number={16},
  volume={587},
  issn={0014-5793},
  journal={FEBS Letters},
  pages={2572--2577},
  author={Wietek, Jonas and Haralampiev, Ivan and Amoussouvi, Aouefa and Herrmann, Andreas and Stöckl, Martin T.}
}
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