Simulations of Ovocleidin-17 Binding to Calcite Surfaces and Its Implications for Eggshell Formation
Simulations of Ovocleidin-17 Binding to Calcite Surfaces and Its Implications for Eggshell Formation
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DOI：
10.1021/jp200145m
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发表时间：
2011-04-28
影响因子：
3.7
通讯作者：
Rodger, P. Mark
中科院分区：
文献类型：
--
作者：
Freeman, Colin L.;Harding, John H.;Rodger, P. Mark
Ovocleidin-17已被确定为一种主要的蛋壳形成蛋白，但其作用和功能仍不确定。用经典的分子动力学方法模拟了卵叶绿素-17蛋白在方解石表面的吸附。对于每种构型，都提供了结合蛋白的详细数据，包括氢键分析、结构检查和吸附能。模拟表明，结合是蛋白质和强结合地表水之间的竞争，因此最有利的构型可以最小化地表水的置换。Ovocleidin-17蛋白相对较硬，与表面接触时结构变化很小，精氨酸残基是方解石表面最重要的结合剂。
Ovocleidin-17 has been identified as a major eggshell-forming protein although the role and function it performs is still uncertain. Classical molecular dynamics simulations are presented for the adsorption of the whole ovocleidin-17 protein onto the {10.4} surface of calcite in several different configurations. For each configuration detailed data are presented of the bound protein with hydrogen-bond analysis, structural examination, and adsorption energies. The simulations demonstrate that binding is a competition between the protein and the strongly bound surface water such that the most energetically favorable configuration minimizes the displacement of this surface water. The ovocleidin-17 protein is found to be relatively rigid, undergoing few structural changes on contact with the surface, and the arginine residues are the most important binders to the calcite surface.