Investigating the Interaction Between Ice-Binding Proteins and Ice Surfaces Using Microfluidic Devices and Cold Stages.

Ice-binding proteins (IBPs) protect organisms living in sub-freezing conditions by inhibiting ice growth in fish and insects, limiting ice recrystallization in plants, and assisting bacteria to adhere to ice. The mechanisms by which these proteins bind to ice and inhibit its growth have been studied both experimentally and using molecular dynamic simulations. A unique experimental technique developed to test and characterize the interactions between IBPs and ice using a combination of a microfluidic device, cold stages with millikelvin temperature resolution, fluorescence-labeled IBPs, and fluorescence microscopy is described herein. The main advantage of this technique is the ability to exchange the solution around micron-sized ice crystals and characterize their binding to and inhibition of ice.