NMR paramagnetic relaxation enhancement experiments were applied to the intrinsically disordered protein α-synuclein, the primary protein in Parkinson's disease, to directly characterize transient intermolecular complexes at neutral and low pH. At neutral pH, we observed weak N- to C-terminal interchain contacts driven by electrostatic interactions, while at low pH, the C- to C-terminal interchain interactions are significantly stronger and driven by hydrophobic contacts. Characterization of these first interchain interactions will provide fundamental insight into the mechanism of amyloid formation.
|Original language||English (US)|
|Number of pages||2|
|Journal||Journal of the American Chemical Society|
|State||Published - Apr 28 2010|
All Science Journal Classification (ASJC) codes
- Colloid and Surface Chemistry