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• W2436008330 startingPage "268" @default.
• W2436008330 abstract "Antifreeze proteins (AFP) observed in cold-adapting organisms bind to ice crystals and prevent further ice growth. However, the molecular mechanism of AFP-ice binding and AFP-inhibited ice growth remains unclear. Here we report the interaction of the insect antifreeze protein (Tenebrio molitor, TmAFP) with ice crystal by molecular dynamics simulation studies. Two sets of simulations were carried out at 263 K by placing the protein near the primary prism plane (PP) and basal plane (BL) of the ice crystal. To delineate the effect of temperatures, both the PP and BL simulations were carried out at 253 K as well. The analyses revealed that the protein interacts strongly with the ice crystal in BL simulation than in PP simulation both at 263 K and 253 K. Further, it was observed that the interactions are primarily mediated through the interface waters. We also observed that as the temperature decreases, the interaction between the protein and the ice increases which can be attributed to the decreased flexibility and the increased structuring of the protein at low temperature. In essence, our study has shed light on the interaction mechanism between the TmAFP antifreeze protein and the ice crystal." @default.
• W2436008330 created "2016-06-24" @default.
• W2436008330 creator A5068778615 @default.
• W2436008330 creator A5090007293 @default.
• W2436008330 date "2016-06-15" @default.
• W2436008330 modified "2023-10-16" @default.
• W2436008330 title "Interaction of<i>Tenebrio Molitor</i>Antifreeze Protein with Ice Crystal: Insights from Molecular Dynamics Simulations" @default.
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• W2436008330 doi "https://doi.org/10.1002/minf.201600034" @default.
• W2436008330 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27492241" @default.
• W2436008330 hasPublicationYear "2016" @default.
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