Dual function of the hydration layer around an antifreeze protein revealed by atomistic molecular dynamics simulations.

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