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Protein binding on stepped calcite surfaces: simulations of ovocleidin-17 on calcite {31.16} and {31.8}

Freeman, C. L., Harding, J. H., Quigley, D. and Rodger, P. M. (2012) Protein binding on stepped calcite surfaces: simulations of ovocleidin-17 on calcite {31.16} and {31.8}. Physical Chemistry Chemical Physics, 14. pp. 7287-7295. ISSN 1463-9076

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Abstract

Simulations using classical molecular dynamics are reported on the binding of the protein Ovocleidin-17 to calcite stepped surfaces. vicinal surfaces ({31.8} and {31.16}) are used to obtain acute and obtuse steps. The simulations demonstrate that binding is greater at the obtuse step. A range of analytical methods is used to show the importance of surface and local water structure for protein binding. We discuss the general features of molecular binding in the light of these results. Our analysis shows that it is unlikely that Ovocleidin-17 is important in controlling crystal morphology; its main role is likely to be in controlling calcite nucleation.

Item Type: Article
Academic Units: The University of Sheffield > Faculty of Engineering (Sheffield) > Department of Materials Science and Engineering (Sheffield)
Depositing User: Dr Colin Freeman
Date Deposited: 18 May 2012 09:37
Last Modified: 08 Feb 2013 17:37
Published Version: http://dx.doi.org/10.1039/c2cp23987f
Status: Published
Publisher: Royal Society of Chemistry
Refereed: Yes
Identification Number: 10.1039/c2cp23987f
URI: http://eprints.whiterose.ac.uk/id/eprint/43898

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