Journal
POLYMER JOURNAL
Volume 44, Issue 7, Pages 690-698Publisher
SPRINGERNATURE
DOI: 10.1038/pj.2012.13
Keywords
crystal growth control; ice-binding protein; ice-water interface; molecular dynamics (MD); thermal hysteresis
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Funding
- Japan Society for the Promotion of Science [21540423]
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) [22107004, 2206]
- Grants-in-Aid for Scientific Research [21540423, 22107004] Funding Source: KAKEN
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Antifreeze proteins (AFPs), which are present in the bodily fluids of organisms inhabiting cold environments, function as inhibitors of ice growth by binding to certain planes of ice crystals. However, the exact mechanism of ice growth inhibition is still poorly understood as it is exceedingly difficult to experimentally analyze the molecular-scale growth kinetics of ice crystals at the planes to which the proteins bind. This review paper focuses on computer simulation studies on the mechanism of ice growth inhibition by AFPs. Recent molecular dynamics simulations of a growing ice-water interface to which protein is bound have indicated that, when the protein is stably bound to the interface, the growth rate of ice surrounding the protein decreases drastically, owing to depression of the ice melting point through the Gibbs-Thomson effect. The observed decrease in growth rate is expected to correspond to ice growth inhibition in real-world systems. In addition to presenting published simulation studies on the mechanism of ice growth inhibition by AFPs, this review also outlines the direction of future simulation studies in this field. Polymer Journal (2012) 44, 690-698; doi: 10.1038/pj.2012.13; published online 14 March 2012
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