Growth suppression of ice crystal basal face in the presence of a moderate ice-binding protein does not confer hyperactivity

Journal:
Proceedings of the National Academy of Sciences of the United States of America
Published:
DOI:
10.1073/pnas.1807461115
Affiliations:
3
Authors:
6

Research Highlight

Chipping away at a new antifreeze protein

© Jeffrey Goodman / Snapwire /Getty

Scientists have observed how proteins inhibit the growth of ice crystals in organisms, which could lead to a wider range of antifreeze applications.

Organisms living in cold climates avoid freezing by producing ice-binding proteins, which attach to ice. Such proteins come into two varieties: a hyperactive type that lowers the freezing point by up to 6 degrees Celsius by attaching to the basal faces of ice crystals, and a moderate type that lowers the freezing point by around 1 degree Celsius by attaching to the prism faces of ice crystals.

Now, researchers from Hokkaido University in Japan have discovered a moderate ice-binding protein outside this classification. It attaches to both the basal and prism faces of ice crystals.

This work sheds new light on how protein molecules interact with ice and could result in new antifreeze applications in the food and medical industries.

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References

  1. Proceedings of the National Academy of Sciences 115, 7479−7484 (2018). doi: 10.1073/pnas.1807461115
Institutions Authors Share
Hokkaido University, Japan
4.000000
0.67
Alfred Wegener Institute - Helmholtz Centre for Polar and Marine Research (AWI), Germany
1.500000
0.25
Lobachevsky State University of Nizhni Novgorod (UNN), Russia
0.500000
0.08