• Journal of the Korean Chemical Society
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• v.62 no.2
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• pp.106-112
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• 2018

Ice-binding proteins have an affinity for ice. They create a gap between the melting and freezing points by inhibiting the growth of ice, known as thermal hysteresis (TH). Interestingly, moderately active LeIBP and hyperactive FfIBP are almost identical in primary and tertiary structures, but differ in TH activity. The TH of FfIBP is tenfold higher than that of LeIBP, due to a subtle difference in their ice-binding motifs. To further evaluate the difference in TH, the interactions were investigated by ice-etching and molecular docking. Ice-etching showed that FfIBP binds to the primary and secondary prism, pyramidal, and basal planes; previously, LeIBP was found to bind to the basal and primary prism planes. Docking analysis using shape complementarity (Sc) showed that the hyperactive FfIBP had higher Sc values for all four ice planes than LeIBP, which is comparable with TH. Docking can be used to describe the hyperactivity of IBPs.

• Journal of the Korean Crystal Growth and Crystal Technology
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• v.5 no.3
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• pp.197-208
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• 1995

An experiment study of the dendrite growth of ice crystals growing in quiescent pure subcooled water was made at small subcoolings of 0.035 K < ${\Delta}T$ < 1.000 K. It was observed that the growth kinetics and morphology are functions of not only subcooling but also thermal convection. When the subcooling is less than 0.35K, it was found that effect of thermal convection on growth kinetics of ice dendrites becomes important. Quantitiative measurements of growth velocity, $V_{G}$, and tip radii of the edge and basal planes, $R_{1}$ and $R_{2}$, were made simultaneously as a function of subcooling.