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Issue 28, 2017
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Room-temperature in-cell EPR spectroscopy: alpha-Synuclein disease variants remain intrinsically disordered in the cell

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Abstract

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.

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

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Publication details

The article was received on 22 May 2017, accepted on 04 Jul 2017 and first published on 04 Jul 2017


Article type: Communication
DOI: 10.1039/C7CP03432F
Citation: Phys. Chem. Chem. Phys., 2017,19, 18147-18151
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    Room-temperature in-cell EPR spectroscopy: alpha-Synuclein disease variants remain intrinsically disordered in the cell

    J. Cattani, V. Subramaniam and M. Drescher, Phys. Chem. Chem. Phys., 2017, 19, 18147
    DOI: 10.1039/C7CP03432F

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