Collet O, Premilat S
Laboratory of Molecular Biophysics, URA CNRS 494, H. Poincaré-Nancy 1 University, Faculty of Sciences, Vandoeuvre les Nancy, France.
Int J Pept Protein Res. 1996 Apr;47(4):239-44. doi: 10.1111/j.1399-3011.1996.tb01351.x.
An efficient Metropolis Monte-Carlo (MMC) procedure is proposed in order to calculate averages of the energy of conformation and structural properties of a polypeptide chain in interaction with a solvent. The contribution of hydration to the free energy of conformation of the macromolecule is calculated using the accessible surface area method. This algorithm, performed with different sets of atomic solvation parameters (ASP), is applied to the peptidic hormone angiotensin II. Different situations of solvation of that molecule are described when the ASP of the polar atoms are fixed to 0, whereas those of the apolar atoms are given values varying from -1.0 to 1.0. From results thus obtained, transitions from extended to collapsed conformations of the polypeptide chain can be simulated. Such changes of conformation could be related to a possible mechanism of binding of this hormone on a membrane surface.
为了计算与溶剂相互作用的多肽链的构象能量平均值和结构性质，提出了一种高效的 metropolis 蒙特卡罗（MMC）程序。使用可及表面积方法计算水合作用对大分子构象自由能的贡献。该算法采用不同的原子溶剂化参数（ASP）集，应用于肽类激素血管紧张素 II。当极性原子的 ASP 固定为 0，而非极性原子的 ASP 取值从 -1.0 到 1.0 时，描述了该分子的不同溶剂化情况。根据由此获得的结果，可以模拟多肽链从伸展构象到折叠构象的转变。这种构象变化可能与该激素在膜表面结合的一种可能机制有关。
