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- W2007331423 endingPage "6202" @default.
- W2007331423 startingPage "6193" @default.
- W2007331423 abstract "Antifreeze proteins (AFPs) are found in different species from polar, alpine, and subarctic regions where they serve to inhibit ice crystal growth by adsorption to ice surfaces. Computational methods have the power to investigate the antifreeze mechanism in atomic detail. Molecular dynamics simulations of water under different conditions have been carried out to test our water model for simulations of biological macromolecules in extreme conditions: very low temperatures (200 K) and at the ice/liquid water interface. We show that the flexible F3C water model reproduces properties of water in the solid phase (ice Ih), the supercooled liquid phase, and at the ice/liquid water interface. Additionally, the hydration of the type III AFP from ocean pout was studied as a function of temperature. Hydration waters on the ice-binding surface of the AFP were less distorted and more tetrahedral than elsewhere on the surface. More ice-like hydrating water structures formed on the ice-binding surface of the protein such that it created an ice-like structure in water within its first hydration layer but not beyond, suggesting that this portion of the protein has high affinity for ice surfaces." @default.
- W2007331423 created "2016-06-24" @default.
- W2007331423 creator A5021239442 @default.
- W2007331423 creator A5025585998 @default.
- W2007331423 date "2008-03-13" @default.
- W2007331423 modified "2023-09-27" @default.
- W2007331423 title "Formation of Ice-like Water Structure on the Surface of an Antifreeze Protein" @default.
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