Simulations of ovocleidin-17 binding to calcite surfaces and its implications for eggshell formation

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 surfac