Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling.

@article{DerSarkissian2003StructuralOO,
  title={Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling.},
  author={Ani Der-Sarkissian and Christine C. Jao and Jeannie Chen and Ralf Langen},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 39},
  pages={37530-5}
}
Despite its importance in Parkinson's disease, a detailed understanding of the structure and mechanism of alpha-synuclein fibril formation remains elusive. In this study, we used site-directed spin labeling and electron paramagnetic resonance spectroscopy to study the structural features of monomeric and fibrillar alpha-synuclein. Our results indicate that monomeric alpha-synuclein, in solution, has a highly dynamic structure, in agreement with the notion that alpha-synuclein is a natively… CONTINUE READING