Suenaga A, Komeiji Y, Uebayasi M, Meguro T, Saito M, Yamato I
Department of Biological Science and Technology, Science University of Tokyo, Chiba, Japan.
Biosci Rep. 1998 Feb;18(1):39-48. doi: 10.1023/a:1022292801256.
The ion permeation process, driven by a membrane potential through an outer membrane protein, OmpF porin of Escherichia coli, was simulated by molecular dynamics. A Na+ ion, initially placed in the solvent region at the outer side of the porin channel, moved along the electric field passing through the porin channel in a 1.3 nsec simulation; the permeation rate was consistent with the experimentally estimated channel activity (10(8)-10(9)/sec). It this simulation, it was indicated that the ion permeation through the porin channel proceeds by a "push-out" mechanism, and that Asp113 is an important residue for the channel activity.
通过分子动力学模拟了由膜电位驱动、通过大肠杆菌外膜蛋白OmpF孔蛋白的离子渗透过程。在一个1.3纳秒的模拟中,最初置于孔蛋白通道外侧溶剂区域的一个Na⁺离子沿着穿过孔蛋白通道的电场移动;渗透速率与实验估计的通道活性(10⁸ - 10⁹/秒)一致。在该模拟中,表明离子通过孔蛋白通道的渗透是通过“推出”机制进行的,并且Asp113是通道活性的一个重要残基。