The crystal growth process by which fish antifreeze proteins (AFPs) and antifreeze glycoproteins (AFGPs) modify the ice morphology is analyzed in the AFP-ice system. A newly identified AFP-induced surface reconstruction mechanism enables one-dimensional helical and irregular globular ice binding surfaces to stabilize secondary, kinetically less stable ice surfaces with variable face indices. Not only are the relative growth rates controlled by the IBS engagement but also the secondary face indices themselves become adjusted in the process of maximizing the AFP-substrate interaction, through attaining the best structural match. The theoretical formulation leads to comprehensive agreement with experiment.
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