Simulations of Ovocleidin-17 Binding to Calcite Surfaces and Its Implications for Eggshell Formation

• Published in: Journal of physical chemistry. C Vol. 115; no. 16; pp. 8175 - 8183
• Main Authors: Freeman, Colin L, Harding, John H, Quigley, David, Rodger, P. Mark
• Format: Journal Article
• Language: English
• Published: American Chemical Society 28.04.2011
• Subjects: C: Surfaces, Interfaces, Catalysis
• ISSN: 1932-7447; 1932-7455
• DOI: 10.1021/jp200145m

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.