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Room-temperature in-cell EPR spectroscopy : alpha-Synuclein disease variants remain intrinsically disordered in the cell

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https://doi.org/10.1039/c7cp03432f
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Physical chemistry chemical physics : PCCP. 2017, 19(28), pp. 18147-18151. ISSN 1463-9084. eISSN 1463-9084. Available under: doi: 10.1039/c7cp03432f

Zusammenfassung

Human alpha-Synuclein (aS), implicated in Parkinson's disease, adopts a rich variety of different conformations depending on the macromolecular context. In order to unravel its pathophysiological role, monitoring its intracellular conformational state and identifying differences for the disease variants is crucial. Here, we present an intracellular spectroscopy approach based on a systematic spin-labeling site-scan in combination with intracellular electron paramagnetic resonance spectroscopy determining conformations on a molecular scale. A quantitative and model-based data analysis revealed that the vast majority of aS, be it wild-type or disease variants A30P or A53T, exists in the monomeric intrinsically disordered form in the cell.

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ISO 690CATTANI, Julia, Vinod SUBRAMANIAM, Malte DRESCHER, 2017. Room-temperature in-cell EPR spectroscopy : alpha-Synuclein disease variants remain intrinsically disordered in the cell. In: Physical chemistry chemical physics : PCCP. 2017, 19(28), pp. 18147-18151. ISSN 1463-9084. eISSN 1463-9084. Available under: doi: 10.1039/c7cp03432f
BibTex
@article{Cattani2017-07-19Roomt-39643,
  year={2017},
  doi={10.1039/c7cp03432f},
  title={Room-temperature in-cell EPR spectroscopy : alpha-Synuclein disease variants remain intrinsically disordered in the cell},
  number={28},
  volume={19},
  issn={1463-9084},
  journal={Physical chemistry chemical physics : PCCP},
  pages={18147--18151},
  author={Cattani, Julia and Subramaniam, Vinod and Drescher, Malte}
}
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