Ice binding proteins (IBPs), also called Œantifreeze proteins‚ or 'ice structuring proteins‚, are a class of proteins that protect organisms from freezing injury. These proteins have many applications in medicine and agriculture, and as a platform for future biotechnology applications. However, the mechanisms underlying the interactions between IBPs and ice surfaces are only partially understood. To elucidate these interactions, and the factors driving IBP activity, we directly visualized fluorescently labeled IBPs on ice crystals in supercooled solutions. This method enabled us to directly examine characteristics such as the kinetics of attachment, ice orientation preference, and thus to assess existing theories for IBP activity. For example we show that the hyperactivity of a class of IBPs stem from their ability to adhere to the basal plan of ice crystals. Further, we develop microfluidic devices for studying ice-proteins systems under both isothermal conditions and with controlled gradients. These microfluidic devices enable us to exchange the solute around the crystals while monitoring the locations and binding kinetics of IBPs and thus opens new avenues for research into ice c
