Structure–Function of IBPs and Their Interactions with Ice

  • Maya Bar-Dolev
  • Koli Basu
  • Ido Braslavsky
  • Peter L. DaviesEmail author


The diversity among the dozen antifreeze proteins (AFPs) and other ice-binding proteins (IBPs) with known or robustly predicted three-dimensional structures is remarkable. Their protein folds range from single short alpha-helices to long beta-solenoids and small globular domains with mixed secondary structure. IBPs differ one from another not only in structure, but also in activity levels, affinity for different ice planes, and ice-binding site size, shape, and amino acid composition. IBPs arose from different evolutionary routes on many different occasions, and even function in different ways to protect the host organism from freeze injury. The only unifying feature of IBPs is their basic function, to bind to ice, and even this is achieved with different orientations and kinetics. This chapter covers the structural diversity of IBPs and their ice-binding sites (IBS). We discuss the correlation between IBS structure and size with activity levels, and how the structural differences are manifested in their binding characteristics. Further we discuss the protein:ice interface at the molecular level and recent mechanisms of ice recognition.


Crystal structure Homology Hyperactive antifreeze Thermal hysteresis Basal plane binding Anchored clathrate waters Compound ice-binding site Quorum of water Ice plane affinity Microfluidics Ice shaping 



This work was supported by grants from the Canadian Institutes of Health Research (P.L.D.) and the Israel Science Foundation (I.B.). P.L.D. holds the Canada Research Chair in Protein Engineering.


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Copyright information

© Springer Nature Switzerland AG 2020

Authors and Affiliations

  • Maya Bar-Dolev
    • 1
  • Koli Basu
    • 2
  • Ido Braslavsky
    • 1
  • Peter L. Davies
    • 2
    Email author
  1. 1.The Hebrew University of JerusalemRehovotIsrael
  2. 2.Queen’s UniversityKingstonCanada

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