Interactions of β-helical antifreeze protein mutants with ice

Maya Bar*, Yeliz Celik, Deborah Fass, Ido Braslavsky

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

40 Scopus citations


The fold of the β-helical antifreeze protein from Tenebrio molitor (TmAFP) proved to be surprisingly tolerant of multiple amino acid substitutions, enabling the construction of a panel of mutants displaying grids of single amino acid types in place of the threonines on the ice-binding face. These mutants, maintaining the regularity of amino acid spacing found in the wild-type protein but with different functional groups on the surface, were tested for antifreeze activity by measuring thermal hysteresis and observing ice grown in their presence. We found that no mutant exhibited the dramatic activity of the wild-type version of this hyperactive antifreeze protein. However, mutants containing four valines or tyrosines in place of the threonines in the center of the TmAFP ice-binding face showed residual thermal hysteresis activity and had marked effects on ice crystal morphology. The results are discussed in the context of a two-stage model for the absorption-inhibition mechanism of antifreeze protein binding to ice surfaces.

Original languageAmerican English
Pages (from-to)2954-2963
Number of pages10
JournalCrystal Growth and Design
Issue number8
StatePublished - Aug 2008
Externally publishedYes


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