Antifreeze proteins (AFP) and glycoproteins (AFGP) help fish, plants, insects and bacteria survive sub-freezing environments. It is well known that these proteins function via some surface interaction, but the exact mechanism has eluded scientists. Aside from mutagenesis experiments directed towards examining the functional importance of specific residues, conclusions about the mechanism have been drawn from indirect studies or more precisely from studies that describe the proteins effects on the ice interface. Here, we will review recent work aimed at directly studying the protein kinetics at the ice interface. fluorescent microscopy is used to determine interaction planes, surface concentrations as well as adsorption characteristics, while fourier transform infra-red attenuated total reflectance (FTIR-ATR) is used to determine the protein structure vs. temperature in the liquid and solid states as well as the ice interface characteristics. Although the functions to some degree are the same, it becomes somewhat evident that the AFGP, AFP III, and spruce budworm AFP (sbwAFP) kinetics at the ice/solution interface, as well as the mechanism, can be rather different.