Go N, Taketomi H
Proc Natl Acad Sci U S A. 1978 Feb;75(2):559-63. doi: 10.1073/pnas.75.2.559.
A lattice model of protein is studied by a Monte Carlo simulation method. The native conformation of the lattice protein molecule is stabilized by specific long-range and short-ranged interactions. By comparing results of simulation for different relative weights of the long- and short-range interactions, it is concluded that the specific long-range interactions are essential for highly cooperative stabilization of the native conformation and that the short-range interactions accelerate the folding and unfolding transitions.
通过蒙特卡罗模拟方法研究了蛋白质的晶格模型。晶格蛋白质分子的天然构象通过特定的长程和短程相互作用得以稳定。通过比较不同长程和短程相互作用相对权重的模拟结果，得出结论：特定的长程相互作用对于天然构象的高度协同稳定至关重要，而短程相互作用加速了折叠和去折叠转变。
