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Updated: Feb 28, 2026

Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity
Published on: January 15, 2014
Effect of antifreeze protein on heterogeneous ice nucleation based on a two-dimensional random-field Ising model
Zhen Dong1, Jianjun Wang2,3, Xin Zhou1
1School of Physical Sciences, University of Chinese Academy of Science, Beijing 100049, People's Republic of China.
Abstract:
Antifreeze proteins (AFPs) are the key biomolecules that protect many species from suffering the extreme conditions. Their unique properties of antifreezing provide the potential of a wide range of applications. Inspired by the present experimental approaches of creating an antifreeze surface by coating AFPs, here we present a two-dimensional random-field lattice Ising model to study the effect of AFPs on heterogeneous ice nucleation. The model shows that both the size and the free-energy effect of individual AFPs and their surface coverage dominate the antifreeze capacity of an AFP-coated surface. The simulation results are consistent with the recent experiments qualitatively, revealing the origin of the surprisingly low antifreeze capacity of an AFP-coated surface when the coverage is not particularly high as shown in experiment. These results will hopefully deepen our understanding of the antifreeze effects and thus be potentially useful for designing novel antifreeze coating materials based on biomolecules.

