The role of Cys179-Cys214 disulfide bond in the stability and folding of prion protein: insights from molecular dynamics simulations.

@article{Ning2014TheRO,
  title={The role of Cys179-Cys214 disulfide bond in the stability and folding of prion protein: insights from molecular dynamics simulations.},
  author={Lulu Ning and Jingjing Guo and Nengzhi Jin and Huanxiang Liu and Xiaojun Yao},
  journal={Journal of molecular modeling},
  year={2014},
  volume={20 2},
  pages={2106}
}
Prion diseases are associated with misfolding and aggregation of prion protein (PrP). Cellular prion protein contains a disulfide bond linking Cys residues at positions 179 and 214. It has been proposed that this disulfide bond plays an important role in the conversion between cellular (PrP(C)) and the scrapie form of prion protein (PrP(Sc)). To probe the role of this disulfide bond in the stability and folding of prion protein, we employed molecular dynamics simulations to study the reduced… CONTINUE READING
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