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.
| Original language | English |
|---|---|
| Pages (from-to) | 18147-18151 |
| Number of pages | 5 |
| Journal | Physical Chemistry Chemical Physics |
| Volume | 19 |
| Issue number | 28 |
| Early online date | 4 Jul 2014 |
| DOIs | |
| Publication status | Published - 28 Jul 2017 |
Funding
This work was financially supported by DFG (SFB 969) as well as the ministry of Science, Research and the Arts of Baden- W?rttemberg (Az 33-7532.20/723). We gratefully acknowledge experimental contributions of Juliane Stehle, Laura Kn?rr, Nathalie Schilderink and Philipp Graus. We thank Martin Spitzbarth for help with data post processing.
| Funders | Funder number |
|---|---|
| Deutsche Forschungsgemeinschaft | SFB 969 |
| Ministerium für Wissenschaft, Forschung und Kunst Baden-Württemberg | Az 33-7532.20/723 |