title: How does an amorphous surface influence molecular binding?--ovocleidin-17 and amorphous calcium carbonate.
abstract: Atomistic molecular dynamics simulations of dehydrated amorphous calcium carbonate interacting with the protein ovocleidin-17 are presented. These simulations demonstrate that the amorphisation of the calcium carbonate surface removes water structure from the surface. This reduction of structure allows the protein to bind with many residues, unlike on crystalline surfaces where binding is strongest when only a few residues are attached to the surface. Basic residues are observed to dominate the binding interactions. The implications for protein control over crystallisation are discussed.
authors.affiliation: Department of Materials Science and Engineering, Sir Robert Hadfield Building, Mappin Street, Sheffield, UK. c.l.freeman@sheffield.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: D001665:Binding Sites; D002119:Calcium Carbonate / Q000737:chemistry*; D004527:Egg Proteins / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D013499:Surface Properties; D014867:Water / Q000737:chemistry
chemical_list: D004527:Egg Proteins; C095273:ovocleidin 17; D014867:Water; D002119:Calcium Carbonate