A pinboard by
Yuqing Qiu

Graduate Student , University of Utah


Size and aggregation of ice binding proteins controls their ice nucleation efficiency.

We use molecular dynamic simulations to demonstrate that the size of ice binding surface in the ice nucleating proteins determines their roles as ice nucleating proteins or antifreeze proteins. We find that increasing the length of ice nucleating protein monomer increases their nucleating ability. The critical ice nucleus on ice nucleating proteins can adapt to the surface and elongate along the ice-binding surface. Ice nucleating protein monomers dimerize with an optimized gap distance of 1.1 ~ 1.2 nm, stabilizing the stacking disordered surface of ice. We predict that the domain of ice nucleating aggregates that nucleate ice at -2 °C contain 25 monomers. We elucidate how the size, shape and dimerization influence the ice nucleating ability of ice-binding proteins. These analyses provide us a strategy to assemble small ice-binding materials to construct super effective ice nucleating agent.