Skinks of the Ctenotus schevilli species group

Volume: 22Start Page: 289End Page: 29

The peregrine falcon (Falco peregrinus macropus) Swainson in southeastern Queensland

Volume: 18Start Page: 81End Page: 9

Taudactylus diurnis and the case of the disappearing frogs

Volume: 29Start Page: 361End Page: 36

A new locality for Litoria brevipalmata (Anura: Pelodryadidae) from south-east Queensland

Volume: 95Start Page: 150End Page: 15

The emerald monitor Varanus prasinus (Schlegel): an addition to the Australian mainland herpetofauna

Volume: 20Start Page: 103End Page: 10

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

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