Molecular dynamics simulation of temperature induced unfolding of animal prion protein.
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.
Institute of Environmental and Analytical Sciences, College of Chemistry and Chemical Engineering, Henan University, Kaifeng, 475001, Henan, China, xin_chen@henu.edu.cn.
Xin
X
Chen
Danhui
D
Duan
Shuyan
S
Zhu
Jinglai
J
Zhang
D000818:Animals; D003411:Arvicolinae; D003553:Cystine / Q000737:chemistry; D006860:Hydrogen Bonding; D056004:Molecular Dynamics Simulation; D018621:PrPC Proteins / Q000737:chemistry*; D017096:Prion Diseases / Q000628:therapy; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D058767:Protein Unfolding; D013816:Thermodynamics; D014426:Turtles
D018621:PrPC Proteins; D003553:Cystine