Issue 26, 2015

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.

Graphical abstract: How does an amorphous surface influence molecular binding? – ovocleidin-17 and amorphous calcium carbonate

Supplementary files

Article information

Article type
Paper
Submitted
23 Jan 2015
Accepted
22 Apr 2015
First published
26 May 2015

Phys. Chem. Chem. Phys., 2015,17, 17494-17500

Author version available

How does an amorphous surface influence molecular binding? – ovocleidin-17 and amorphous calcium carbonate

C. L. Freeman, J. H. Harding, D. Quigley and P. M. Rodger, Phys. Chem. Chem. Phys., 2015, 17, 17494 DOI: 10.1039/C5CP00434A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements