Molecular dynamics simulation of temperature induced unfolding of animal prion protein
Molecular dynamics simulation of temperature induced unfolding of animal prion protein
复制标题
温度诱导动物朊病毒蛋白去折叠的分子动力学模拟
DOI：
10.1007/s00894-013-1955-0
复制
发表时间：
2013-10-01
影响因子：
2.2
通讯作者：
Zhang, Jinglai
中科院分区：
文献类型：
--
作者：
Chen, Xin;Duan, Danhui;Zhang, Jinglai
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 α-helix was more stable than β-sheet. Extension and disruption of β-sheet commonly appeared in the temperature induced unfolding process. The conversion of α-helix to π-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.FigureMolecular dynamics simulation of temperature induced unfolding of animal prion protein
