Simulations of Ovocleidin-17 Binding to Calcite Surfaces and Its Implications for Eggshell Formation
| Autor: | David Quigley, P. Mark Rodger, Colin L. Freeman, John H. Harding |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Calcite
Surface (mathematics) Ovocleidin 17 Eggshell formation Surfaces Coatings and Films Electronic Optical and Magnetic Materials chemistry.chemical_compound Crystallography Molecular dynamics General Energy Adsorption chemistry Chemical physics Physical and Theoretical Chemistry Displacement (fluid) Surface water |
| Zdroj: | The Journal of Physical Chemistry C. 115:8175-8183 |
| ISSN: | 1932-7455 1932-7447 |
| DOI: | 10.1021/jp200145m |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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