Structure-function of IBPs and their interactions with ice

Maya Bar-Dolev, Koli Basu, Ido Braslavsky, Peter L. Davies*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

9 Scopus citations


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.

Original languageAmerican English
Title of host publicationAntifreeze Proteins Volume 2
Subtitle of host publicationBiochemistry, Molecular Biology and Applications
PublisherSpringer International Publishing
Number of pages39
ISBN (Electronic)9783030419486
ISBN (Print)9783030419479
StatePublished - 1 Jan 2020

Bibliographical note

Publisher Copyright:
© Springer Nature Switzerland AG 2020.


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


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