Okamoto Y, Kikuchi T, Nakazawa T, Kawai H
Department of Physics, Nara Women's University, Japan.
Int J Pept Protein Res. 1993 Sep;42(3):300-3. doi: 10.1111/j.1399-3011.1993.tb00146.x.
Tertiary structure of parathyroid hormone fragment (1-34) is predicted by the Monte Carlo simulated annealing method. Among the 20 structures obtained after completely unbiased calculations, the lowest-energy conformation exhibits two alpha-helices around residues 2-10 and 18-22. This structure agrees with the models, especially with the location of helices, deduced from experiments. In addition, the simulation supports empirical implications in the following two points. (1) The helix near the N-terminus is more stable than the C-terminal one. (2) The rest of the peptide segments are flexible and do not tend to have any definite structure. Our calculation correctly predicts only an alpha-helix, whereas previous analyses by the Chou-Fasman method leave an ambiguity between an alpha-helix and a beta-strand.
采用蒙特卡罗模拟退火方法预测甲状旁腺激素片段（1-34）的三级结构。在完全无偏计算后获得的20种结构中，能量最低的构象在残基2-10和18-22周围呈现出两个α-螺旋。该结构与从实验推导的模型相符，特别是螺旋的位置。此外，模拟在以下两点支持经验性结论。（1）靠近N端的螺旋比C端的螺旋更稳定。（2）肽段的其余部分是灵活的，且不倾向于具有任何确定的结构。我们的计算仅正确预测了一个α-螺旋，而先前用Chou-Fasman方法进行的分析在α-螺旋和β-链之间存在歧义。
