Accessibility navigation


Function of the hydration layer around an antifreeze protein revealed by atomistic molecular dynamics simulations

Nutt, D.R. and Smith, J.C. (2008) Function of the hydration layer around an antifreeze protein revealed by atomistic molecular dynamics simulations. Journal of the American Chemical Society, 130 (39). pp. 13066-13073. ISSN 0002-7863

Full text not archived in this repository.

To link to this article DOI: 10.1021/ja8034027

Abstract/Summary

Atomistic molecular dynamics simulations are used to investigate the mechanism by which the antifreeze protein from the spruce budworm, Choristoneura fumiferana, binds to ice. Comparison of structural and dynamic properties of the water around the three faces of the triangular prism-shaped protein in aqueous solution reveals that at low temperature the water structure is ordered and the dynamics slowed down around the ice-binding face of the protein, with a disordering effect observed around the other two faces. These results suggest a dual role for the solvation water around the protein. The preconfigured solvation shell around the ice-binding face is involved in the initial recognition and binding of the antifreeze protein to ice by lowering the barrier for binding and consolidation of the protein:ice interaction surface. Thus, the antifreeze protein can bind to the molecularly rough ice surface by becoming actively involved in the formation of its own binding site. Also, the disruption of water structure around the rest of the protein helps prevent the adsorbed protein becoming covered by further ice growth.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11537
Uncontrolled Keywords:LIQUID WATER, ICE/WATER INTERFACE, POTENTIAL FUNCTIONS, ANTARCTIC FISHES, ICE NUCLEATION, RANDOM NETWORK, MODEL, MECHANISM, BINDING, SURFACE
Publisher:American Chemical Society

Centaur Editors: Update this record

Page navigation