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Mixing antifreeze protein types changes ice crystal morphology without affecting antifreeze activity
Author(s) -
Heman Chao,
DeLuca Carl I.,
Davies Peter L.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01357-7
Subject(s) - antifreeze protein , antifreeze , ice crystals , morphology (biology) , chemistry , mixing (physics) , biophysics , chemical engineering , biochemistry , biology , zoology , organic chemistry , physics , meteorology , quantum mechanics , engineering
All three fish antifreeze protein types (I, II and III) inhibit the growth of ice to form hexagonal bipyramidal ice crystals of characteristic morphology. Mixtures of these different antifreezes produced ice crystals of hybrid shapes and dimensions, consistent with the different antifreeze types binding to the same ice surfaces. The activity of the mixtures was independent of the proportions of the iso‐active antifreeze protein stocks present, indicating that the different antifreezes neither attenuated nor potentiated each other's activity. We suggest that antifreeze protein molecules are independently active and do not require protein‐protein interactions for ice‐binding.