Freeman, Colin L., Harding, John H., Quigley, David (Researcher in physics) and Rodger, P. Mark. (2012) Protein binding on stepped calcite surfaces : simulations of ovocleidin-17 on calcite {31.16} and {31.8}. Physical Chemistry Chemical Physics, Vol.14 (No.20). 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. © 2012 the Owner Societies.

Item Type:	Journal Article
Divisions:	Faculty of Science > Chemistry Faculty of Science > Physics Faculty of Science > Centre for Scientific Computing
Journal or Publication Title:	Physical Chemistry Chemical Physics
Publisher:	Royal Society of Chemistry
ISSN:	1463-9076
Official Date:	28 May 2012
Volume:	Vol.14
Number:	No.20
Page Range:	pp. 7287-7295
Identification Number:	10.1039/c2cp23987f
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
URI:	http://wrap.warwick.ac.uk/id/eprint/49414

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