Paper Citing NAMD - Abstract
Hu, Guodong; Qi, Lisheng; Dou, Xianghua; Wang, Jihua
The influences of protonation state of histidine on aromatic/arginine region of aquaporin-1 protein
MOLECULAR SIMULATION, 39:261-269, APR 1 2013
Aquaporin-1 (AQP1) is widely distributed in the epithelial tissue for water absorption and secretion. The histidine (His182) residue in the aromatic/arginine (ar/R) constriction region plays an important role in transporting water through the membrane. In this study, we have performed a total of 46ns equilibrium molecular dynamics (MD) simulations, and obtained the influence of His182 in two protonation states (Hsd is the proton at N and Hse is the proton at NE) on the ar/R region. Water permeation rate shows that it is easier for water molecules to permeate the ar/R region of the AQP1 with residue in the Hsd state than in the Hse state. The minimum radii of the pore in the ar/R region were calculated during the last 10ns MD simulation. We have analysed the correlation among the state of the pore (open or close), the minimum radius of the ar/R region and the dihedral angles
