抗冻蛋白
冰核
冰晶
化学
同种类的
成核
无定形冰
过冷
化学物理
结晶学
生物物理学
化学工程
生物
热力学
生物化学
物理
有机化学
无定形固体
气象学
工程类
作者
Lukas Eickhoff,Katharina Dreischmeier,Assaf Zipori,Vera Sirotinskaya,Chen Adar,Nàama Reicher,Ido Braslavsky,Yinon Rudich,Thomas Koop
标识
DOI:10.1021/acs.jpclett.8b03719
摘要
Several types of natural molecules interact specifically with ice crystals. Small antifreeze proteins (AFPs) adsorb to particular facets of ice crystals, thus inhibiting their growth, whereas larger ice-nucleating proteins (INPs) can trigger the formation of new ice crystals at temperatures much higher than the homogeneous ice nucleation temperature of pure water. It has been proposed that both types of proteins interact similarly with ice and that, in principle, they may be able to exhibit both functions. Here we investigated two naturally occurring antifreeze proteins, one from fish, type-III AFP, and one from beetles, TmAFP. We show that in addition to ice growth inhibition, both can also trigger ice nucleation above the homogeneous freezing temperature, providing unambiguous experimental proof for their contrasting behavior. Our analysis suggests that the predominant difference between AFPs and INPs is their molecular size, which is a very good predictor of their ice nucleation temperature.
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