Abstract
The ability of antifreeze proteins (AFPs) to depress a freezing point without affecting the equilibrium melting point remains a mystery. This disparity between freezing and melting point is also known as thermal hysteresis. Previous Molecular Dynamic (MD) studies have found that the glycoprotein AFP variants bind to ice predominantly through hydrophobic resides but there are other classes of AFP without sugar structural components. DAFP-1 is an AFP found in a Dendroides canadensis species of beetle, consisting of 83 amino acid residues bound together in a helical shape by disulfide bridges, and lacking a sugar component. Using biased molecular dynamics, we are simulating DAFP-1 at ice/water interfaces and characterizing the free energy profile. This is done by rotating the protein using a biasing potential and then working backwards to the unbiased free energy using umbrella sampling. By characterizing the side chain interactions with both the water and the ice we hope to illustrate the binding interactions contributing to the freezing point depression for AFPs without sugar components. We can then use the free energy profile improve the overall understanding of AFP to thermal hysteresis.
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