Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes.

@article{Davidson1998StabilizationOA,
  title={Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes.},
  author={W. Sean Davidson and Ana Jonas and David F. Clayton and Julia M. George},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 16},
  pages={9443-9}
}
alpha-Synuclein is a highly conserved presynaptic protein of unknown function. A mutation in the protein has been causally linked to Parkinson's disease in humans, and the normal protein is an abundant component of the intraneuronal inclusions (Lewy bodies) characteristic of the disease. alpha-Synuclein is also the precursor to an intrinsic component of extracellular plaques in Alzheimer's disease. The alpha-synuclein sequence is largely composed of degenerate 11-residue repeats reminiscent of… CONTINUE READING
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