Belorusskiĭ L A
Mol Biol (Mosk). 1976 Nov-Dec;10(6):1341-8.
Variation of ribonuclease S structure is analysed with the potential energy being minimized by a computer. The function of potential energy contains the potentials of bond and angle distortions, torsional and non-valent interactions. It is shown that after 100 iterations the potential energy is decreased from the value of 6500 kcal/mole to--1012 kcal/mole, 92% of complete change of energy fitting the first ten iterations. The root mean square deviation (r. ms. d.) of final structure from the initial one is 0.232 A (0.206 A for the backbone and 0.257 A for side groups). The forbidden non-valent contacts are completely removed after minimization. R. ms. d. of the equilibrium value is decreased from 0.097 to 0.006 A for bond lengths; from 7.660 to 3.65 degrees for valence an-les and from 9.44 to 6.95 degrees for rotation angles around the peptide bonds. Distribution of tensions along the protein chain after minimization is considerably changed, the tensions decreasing in average by 100 times.
通过计算机将核糖核酸酶S结构的势能最小化，对其结构变化进行了分析。势能函数包含键和角畸变、扭转和非价相互作用的势能。结果表明，经过100次迭代后，势能从6500千卡/摩尔降至-1012千卡/摩尔，能量的完全变化中有92%在前十次迭代中拟合。最终结构与初始结构的均方根偏差（r.ms.d.）为0.232埃（主链为0.206埃，侧链为0.257埃）。最小化后，禁止的非价接触完全消除。键长的平衡值的均方根偏差从0.097降至0.006埃；价角从7.660度降至3.65度，肽键周围的旋转角从9.44度降至6.95度。最小化后，沿蛋白质链的张力分布发生了显著变化，张力平均降低了100倍。
