@article{d8a5e5f074c211dbbee902004c4f4f50,
title = "Mapping Long-Range Interactions in a-Synuclein using Spin-Label NMR and Ensemble Molecular Dynamics Simulations",
abstract = "The intrinsically disordered protein a-synuclein plays a key role in the pathogenesis of Parkinson's disease (PD). We show here that the native state of a-synuclein consists of a broad distribution of conformers with an ensemble-averaged hydrodynamic radius significantly smaller than that expected for a random coil structure. This partial condensation is driven by interactions between the highly charged C-terminus and a large hydrophobic central region of the protein sequence. We suggest that this structure could inhibit the formation of a-synuclein aggregates, which are thought to be the cytotoxic species responsible for neurodegeneration in PD.",
author = "Dedmon, {M. M.} and K. Lindorff-Larsen and J. Christodoulou and Michele Vendruscolo and Dobson, {C. M.}",
year = "2005",
doi = "10.1021/ja044834j",
language = "English",
volume = "127",
pages = "476--477",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "ACS Publications",
number = "2",
}