Noguti T, Go N
Computation Center, Faculty of Engineering, Kyushu University, Fukuoka, Japan.
Proteins. 1989;5(2):113-24. doi: 10.1002/prot.340050205.
An analysis is carried out of differences in the minimum energy conformations obtained in the previous paper by energy minimization starting from conformations sampled by a Monte Carlo simulation of conformational fluctuations in the native state of a globular protein, bovine pancreatic trypsin inhibitor. Main conformational differences in each pair of energy minima are found usually localized in several side chains and in a few local main chain segments. Such side chains and local main chain segments are found to take a few distinct local conformations in the minimum energy conformations. Energy minimum conformations can thus be described in terms of combinations of these multiple local conformations.
对前一篇论文中通过能量最小化获得的最低能量构象的差异进行了分析，能量最小化是从球状蛋白牛胰蛋白酶抑制剂天然状态下构象波动的蒙特卡罗模拟所采样的构象开始的。发现每对能量最小值中的主要构象差异通常定位在几个侧链和少数局部主链片段中。发现这些侧链和局部主链片段在最低能量构象中采取几种不同的局部构象。因此，最低能量构象可以用这些多个局部构象的组合来描述。
