Hydration behavior at the ice-binding surface of the Tenebrio molitor antifreeze protein.

Abstract

Molecular dynamics (MD) simulations have been carried out at two different temperatures (300 and 220 K) to study the conformational rigidity of the hyperactive Tenebrio molitor antifreeze protein (TmAFP) in aqueous medium and the structural arrangements of water molecules hydrating its surface. It is found that irrespective of the temperature the ice… (More)
DOI: 10.1021/jp412528b

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@article{Midya2014HydrationBA, title={Hydration behavior at the ice-binding surface of the Tenebrio molitor antifreeze protein.}, author={Uday Sankar Midya and Sanjoy Bandyopadhyay}, journal={The journal of physical chemistry. B}, year={2014}, volume={118 18}, pages={4743-52} }