The antifreeze protein (AFP) activity is explained using two models. The first model is using ice binding and the second is using antiice structuralization of water molecules. The description of AFP function using anti-ice structuralization of water molecules is less explored. Therefore, it is of interest to explain AFP function using this model. Protein folding is often described using models where hydrophobic residues move away from water getting buried and hydrophilic residues are exposed to the surface. Thus, the 3D Gauss function stretched on the protein molecule describes the hydrophobicity distribution in a protein molecule. Small antifreeze proteins (less than 150 residues) are often represented by structures with hydrophobic core. Large antifreeze proteins (above 200 residues) contain solenoid (modular repeats). The hydrophobic field of solenoid show different distribution with linear propagation of the bands of different hydrophobicity level having high and low hydrophobicity that is propagated parallel to the long axis of solenoid. This specific ordering of hydrophobicity implies water molecules ordering different from ice. We illustrate this phenomenon using two antifreeze proteins to describe the hypothesis.
Keywords: activity; anti-ice; antifreeze proteins; function; ice; models.