Noguti T, Go N, Ooi T, Nishikawa K
Biochim Biophys Acta. 1981 Nov 30;671(1):93-8. doi: 10.1016/0005-2795(81)90098-2.
The conformation energy surface of a small protein, basic pancreatic trypsin inhibitor, is studied to characterize small-amplitude thermal fluctuations in the protein molecule. In order to see the shape of the conformational energy surface near the energy minimum point, the thermal equilibrium of the molecule is stimulated by the Monte Carlo method of Metropolis et al. From the sample of the equilibrium population, which reflects the shape of the energy surface, orthogonal directions are generated in the conformational space, and the conformational energy is actually calculated along these directions. All energy profiles along these directions are found to be approximately a parabola within the range of thermal fluctuations, which suggests the possibility of harmonic approximation to the conformational energy surface of the globular protein.
研究了一种小蛋白质——碱性胰蛋白酶抑制剂的构象能面，以表征蛋白质分子中的小幅度热涨落。为了观察能量最低点附近构象能面的形状，采用Metropolis等人的蒙特卡罗方法来模拟分子的热平衡。从反映能面形状的平衡总体样本中，在构象空间生成正交方向，并沿这些方向实际计算构象能。发现在热涨落范围内，沿这些方向的所有能量分布近似为抛物线，这表明对球状蛋白质的构象能面进行简谐近似是可能的。
