Observation of ice-like water layers at an aqueous protein surface

K. Meister, Simona Strazdaite, Arthur L. DeVries, Stephan Lotze, Luuk L.C. Olijve, Ilja K. Voets, Huib J. Bakker

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We study the properties of water at the surface of an antifreeze protein with femtosecond surface sum frequency generation spectroscopy. We find clear evidence for the presence of ice-like water layers at the ice-binding site of the protein in aqueous solution at temperatures above the freezing point. Decreasing the temperature to the biological working temperature of the protein (0°C to -2°C) increases the amount of ice-like water, while a single point mutation in the ice-binding site is observed to completely disrupt the ice-like character and to eliminate antifreeze activity. Our observations indicate that not the protein itself but ordered ice-like water layers are responsible for the recognition and binding to ice.

Original languageEnglish
Pages (from-to)17732-17736
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America (PNAS)
Issue number50
Publication statusPublished - 16 Dec 2014


  • Antifreeze proteins
  • Protein hydration
  • Sum frequency generation


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