title: Protein binding on stepped calcite surfaces: simulations of ovocleidin-17 on calcite {31.16} and {31.8}.
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.
authors.affiliation: Department of Materials Science and Engineering, Sir Robert Hadfield Building, Mappin Street, Sheffield, UK. c.l.freeman@shef.ac.uk
authors.forename: Colin L
authors.initials: CL
authors.lastname: Freeman
authors.forename: John H
authors.initials: JH
authors.lastname: Harding
authors.forename: David
authors.initials: D
authors.lastname: Quigley
authors.forename: P Mark
authors.initials: PM
authors.lastname: Rodger
mesh_terms: D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D002119:Calcium Carbonate / Q000737:chemistry / Q000378:metabolism*; D002645:Chickens; D004527:Egg Proteins / Q000737:chemistry / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D013499:Surface Properties
chemical_list: D000596:Amino Acids; D004527:Egg Proteins; C095273:ovocleidin 17; D002119:Calcium Carbonate