A computer simulation of the spruce budworm antifreeze proteins and ice. Kuiper et al. (2015) (CC BY 4.0)

How do antifreeze proteins work?

Computer simulations reveal how an insect’s antifreeze protein stops ice crystals from growing.

Water expands as it freezes. If this happens to the water inside plants and animals, the resulting ice crystals can rupture cells. To prevent this, many plants and animals that live in cold climates have evolved ‘antifreeze proteins’. When a small particle of ice first starts to form, the antifreeze proteins bind to it and prevent the water around it freezing, hence preventing the growth of an ice crystal.

There are many different types of antifreeze protein, and some are more active than others. For example, some insects including the spruce budworm are exposed to extremely cold temperatures — sometimes below −30°C — and these insects have antifreeze proteins that are highly active.

It is not fully understood how different antifreeze proteins interact with ice and prevent the growth of ice crystals. This is largely because, as yet, there are no experimental techniques that make it possible to see how antifreeze proteins and water molecules arrange themselves at the surface of a growing particle of ice. Instead, scientists have developed computer simulations to investigate this process. While many of these studies have provided valuable information, the computational methods used have only recently become powerful enough to analyze how the antifreeze proteins approach the surface of the ice particle.

Michael Kuiper and colleagues carried out simulations involving a highly active antifreeze protein from the spruce budworm. The results of these simulations revealed that this antifreeze protein does not bind directly to ice; instead, water molecules at the surface of the protein act as a bridge between the protein and the ice. These water molecules are highly ordered and though they have similarities with how water is structured in the ice, they are distinct from the ice lattice itself. Furthermore, this arrangement appears to be important for allowing the spruce budworm antifreeze protein to interact with the ice.

This study provides detailed insights as to how a highly active antifreeze protein helps to prevent ice crystals forming. In the future, the computational simulations used here may be extended to study the dynamics of other antifreeze proteins, and also how crystals of other materials form.

To find out more

Read the eLife research paper on which this eLife Digest is based: “The biological function of an insect antifreeze protein simulated by molecular dynamics” (May 7, 2015).

eLife is an open-access journal that publishes outstanding research in the life sciences and biomedicine.

The main text on this page was reused (with modification) under the terms of a Creative Commons Attribution 4.0 International License. The original “eLife digest” can be found in the linked eLife research paper.