Ice possesses the ability to align water molecules, hence attracting the nearby water molecules to form an ice layer too i.e. to make it frozen too. However, in organisms residing in chilled habitats, there is a potent antifreeze protein which enables to loosen the grip of ice on water.
Lately, an article titled “Molecular structure of a hyperactive antifreeze protein adsorbed to ice” published in ‘The Journal of chemical physics’, focused on examining deeply the molecular structure of that powerful antifreeze protein & comprehending how it works. Konrad Meister & his team has traveled to world’s coldest places inclusive of Arctic & Antarctica, to gather antifreeze protein from various sources.
Meister stated about the protein that “The antifreeze proteins have one side that is uniquely structured, the so-called ice-binding site of the protein, which is very flat, slightly hydrophobic and doesn’t have any charged residues. But how this side is used to interact with ice is obviously very difficult to understand if you can’t measure an ice-protein interface directly.”
Scientists absorbed these distinctive biomolecules into the laboratory’ ice to closely inspect the mechanisms that lead to the interaction when antifreeze proteins are in touch with ice.
Researchers discovered that when these molecules get in touch with ice, rather than getting the freeze, the molecules of water are changed to have a completely different chemical structure & orientation. Meister added: “Molecular-scale information is the key to understanding the function or the working mechanism of antifreeze proteins, and if we know that, then we can start making something cool that we as a society can benefit from.”
This unique antifreeze characteristic could be employed as a model for developing synthetic versions which would help to remove ice from airplanes, prevention of crystal formation on ice cream in the freezer & for protecting organs.
Meister further said: “This is the first time we’ve put biomolecules on ice. Bringing experts from different fields together was really the big step forward in this case because the entire problem is very interdisciplinary.”