Paper Citing NAMD - Abstract
Chen, Xin; Duan, Danhui; Zhu, Shuyan; Zhang, Jinglai
Molecular dynamics simulation of temperature induced unfolding of animal prion protein
JOURNAL OF MOLECULAR MODELING, 19:4433-4441, OCT 2013
To elucidate the structural stability and the unfolding dynamics of the animal prion protein, the temperature induced structural evolution of turtle prion protein (tPrPc) and bank vole prion protein (bvPrPc) have been performed with molecular dynamics (MD) simulation. The unfolding behaviors of secondary structures showed that the alpha-helix was more stable than beta-sheet. Extension and disruption of beta-sheet commonly appeared in the temperature induced unfolding process. The conversion of alpha-helix to pi-helix occurred more readily at the elevating temperature. Furthermore, it was suggested in this work that the unfolding of prion protein could be regulated by the temperature.
