How do antifreeze proteins inhibit Ostwald ripening of ice crystals?:analyzing local surface curvature changes at high resolution

Many lifeforms produce ice-binding proteins, sometimes referred to as antifreeze proteins, that can protect them against frost-damage by controlling the nucleation and growth of ice crystals. Our goal is to elucidate how these proteins can modulate the water-ice phase transition and function as such remarkable cryo-protectants. Specifically, we seek to directly resolve how antifreeze proteins dynamically organize at the solid-liquid interface and interact with advancing ice-crystal planes. To this end, we have developed a new experimental approach that is suited for high-resolution imaging of ice crystals and for fluorescence microscopy for localization of single proteins. We perform quantitative analyses of the Ostwald ripening process in absence and presence of antifreeze proteins where we examine the local and global evolution of the system. Novel image-analysis algorithms have been developed that are capable of extracting the local curvature of ice crystals for quantitative analysis of the boundaries evolution and their pinning due to binding of the proteins. These analyses aim to elucidate crystal-plane specific ice recrystallization and its inhibition by ice-binding proteins