The N-terminus of the intrinsically disordered protein α-synuclein triggers membrane binding and helix folding.

@article{Bartels2010TheNO,
  title={The N-terminus of the intrinsically disordered protein α-synuclein triggers membrane binding and helix folding.},
  author={Tim Bartels and Logan S. Ahlstrom and Avigdor Leftin and Frits Kamp and Christian Haass and Michael F Brown and Klaus D Beyer},
  journal={Biophysical journal},
  year={2010},
  volume={99 7},
  pages={2116-24}
}
Alpha-synuclein (αS) is a 140-amino-acid protein that is involved in a number of neurodegenerative diseases. In Parkinson's disease, the protein is typically encountered in intracellular, high-molecular-weight aggregates. Although αS is abundant in the presynaptic terminals of the central nervous system, its physiological function is still unknown. There is strong evidence for the membrane affinity of the protein. One hypothesis is that lipid-induced binding and helix folding may modulate the… CONTINUE READING