Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions

Nat Biotechnol. 2006 Jul;24(7):852-5. doi: 10.1038/nbt1224. Epub 2006 Jul 2.


Antifreeze proteins (AFPs) are found in cold-adapted organisms and have the unusual ability to bind to and inhibit the growth of ice crystals. However, the underlying molecular basis of their ice-binding activity is unclear because of the difficulty of studying the AFP-ice interaction directly and the lack of a common motif, domain or fold among different AFPs. We have formulated a generic ice-binding model and incorporated it into a physicochemical pattern-recognition algorithm. It successfully recognizes ice-binding surfaces for a diverse range of AFPs, and clearly discriminates AFPs from other structures in the Protein Data Bank. The algorithm was used to identify a novel AFP from winter rye, and the antifreeze activity of this protein was subsequently confirmed. The presence of a common and distinct physicochemical pattern provides a structural basis for unifying AFPs from fish, insects and plants.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Antifreeze Proteins / classification
  • Antifreeze Proteins / isolation & purification*
  • Databases, Protein / classification*
  • Models, Chemical
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship


  • Antifreeze Proteins

Associated data

  • GENBANK/DQ641934
  • GENBANK/DQ641935