Ice-binding proteins that accumulate on different ice crystal planes produce distinct thermal hysteresis dynamics.

ABSTRACT: Ice-binding proteins that aid the survival of freeze-avoiding, cold-adapted organisms by inhibiting the growth of endogenous ice crystals are called antifreeze proteins (AFPs). The binding of AFPs to ice causes a separation between the melting point and the freezing point of the ice crystal (thermal hysteresis, TH). TH produced by hyperactive AFPs is an order of magnitude higher than that produced by a typical fish AFP. The basis for this difference in activity remains unclear. Here, we have compared the time dependence of TH activity for both hyperactive and moderately active AFPs using a custom-made nanolitre osmometer and a novel microfluidics system. We found that the TH activities of hyperactive AFPs were time-dependent, and that the TH activity of a moderate AFP was almost insensitiv

SUBMITTER: Drori R 

PROVIDER: S-EPMC4233703 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature