Molecular Evolution of Leucosporidium-derived ice-binding protein (LeIBP)
발표자
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초록
내용
Ice-etching experiment and molecular docking demonstrated that Leucosporidium - derived ice-binding protein (LeIBP) from artic yeast, shows suppression of the growth and re-crystallization of ice, leading to a thermal hysteresis (TH). The ice binding site composed of Thr, Ala, and Ser present in LeIBP binds the protein to ice and inhibits the growth of ice crystals. In this study, the mechanism by which the ice binding site inhibits ice crystal growth is analyzed through molecular dynamics simulation by performing residue mutation of the ice binding site.we also observed the difference in Gibbs-thomson effect in each mutant protein. Additionally, we observed LeIBP from a molecular evolution perspective.