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Journal of the Korean Chemical Society (JKCS)

ISSN 1017-2548(Print)
ISSN 2234-8530(Online)
Volume 62, Number 2
JKCSEZ 62(2)
April 20, 2018 

Evaluation of Thermal Hysteresis Activity of Ice-binding Proteins Using Ice-etching and Molecular Docking
Wahyu Sri Kunto Nugroho, Sangwook Wu, Hak Jun Kim*
Ice-binding protein, Thermal hysteresis, Ice crystal planes, Docking, Shape complementarity
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.
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