Paper Citing NAMD - Abstract
Chen, Xin; Zhu, Shuyan; Wang, Shoubin; Yang, Dagang; Zhang, Jinglai
Molecular dynamics study on the stability of wild-type and the R220K mutant of human prion protein
MOLECULAR SIMULATION, 40:504-513, MAY 3 2014
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases related to the structure transition of -helix into -sheet. In order to gain more direct insight into the molecular basis of the disease, the stability of the wild-type human prion protein (hPrPc) and the R220K mutant (m-hPrPc) was studied by molecular dynamics (MD) and flow MD simulation. Both the thermodynamic stability and the mechanical properties of hPrPc were investigated in this work. It was found that -sheet was more readily to be unfolded in m-hPrPc. In the case of hPrPc, less content of helix was preserved after water turbulence. The H-bond network formed by the mutation-related residue 220 was found to play a key role in the stability of hPrPc.
