Significance: In the past decades, a vast body of experimental and theoretical work has been undertaken to investigate the molecular level mechanism underlying heterogeneous ice nucleation. However, understanding of heterogeneous ice nucleation is still far from satisfactory. Antifreeze proteins (AFPs) are endowed with the unique ability to control freezing. Our research reveals the exact effect of AFPs on ice nucleation at the molecular level, which correlates ice nucleation with the surface chemistry and topography of different faces of AFPs. We also emphasize a critical role for the non–ice-binding face of AFPs and discover that the proper function of AFPs is realized only by synergistic effects of the non–ice-binding face and the ice-binding face.

An ordered water bilayer structure was identified on a rutile TiO₂(110) surface at ambient temperature by combining VSFG experiments and MD simulations, which well explained the long-time controversy on the wetting behaviors of the TiO₂ surface.

The thermal transfer across Pd-H₂O interface is dependent on water structure, where the partial ordered water structure rises the interfacial thermal conductance.