Antifreeze proteins: an unusual receptor-ligand interaction

Trends Biochem Sci. 2002 Feb;27(2):101-6. doi: 10.1016/s0968-0004(01)02028-x.


Antifreeze proteins (AFPs) help organisms to survive below 0 degrees C by inhibiting ice growth. Although AFPs are structurally diverse, they typically present a large proportion of their surface area for binding to ice. Whereas earlier proposed binding mechanisms relied almost entirely on a hydrogen bond match between the AFP and ice, it now seems probable that van der Waals and hydrophobic interactions make a significant contribution to the enthalpy of adsorption. These interactions require intimate surface-surface complementarity between the receptor (AFP) and its ligand (ice).

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antifreeze Proteins / chemistry
  • Antifreeze Proteins / metabolism*
  • Binding Sites
  • Fishes / physiology
  • Insecta / physiology
  • Ligands
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Secondary
  • Structure-Activity Relationship


  • Antifreeze Proteins
  • Ligands