期刊
JOURNAL OF PHYSICAL CHEMISTRY C
卷 115, 期 16, 页码 8175-8183出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp200145m
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资金
- EPSRC [GR/S80103/01, GR/S80127/01, EP/IOO1514/1, EP/F055471/1]
- Engineering and Physical Sciences Research Council [GR/S80103/01, EP/F054785/1, EP/F055471/1, GR/S80127/01, EP/I001514/1] Funding Source: researchfish
- EPSRC [EP/F054785/1, EP/I001514/1, EP/F055471/1] Funding Source: UKRI
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.
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