Antifreeze Proteins Bind Independently to Ice

It has been suggested that cooperative interactions between antifreeze proteins (AFPs) on the ice surfaces are required for complete inhibition of ice crystal growth. To test this hypothesis, a 7-kDa type III AFP was linked through its N-terminus to thioredoxin (12 kDa) or maltose-binding protein (4...

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Bibliographic Details
Published in:Biophysical journal 1998-03, Vol.74 (3), p.1502-1508
Main Authors: DeLuca, Carl I., Comley, Rebecca, Davies, Peter L.
Format: Article
Language:English
Subjects:
Antifreeze Proteins
Base Sequence
Binding Sites
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Freezing
Genes, Synthetic
Glycoproteins - chemistry
Glycoproteins - metabolism
Ice
Maltose-Binding Proteins
Models, Molecular
Oligodeoxyribonucleotides
Protein Binding
Protein Conformation
Protein Structure, Secondary
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - metabolism
Surface Properties
Thioredoxins - chemistry
Thioredoxins - metabolism
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Summary:It has been suggested that cooperative interactions between antifreeze proteins (AFPs) on the ice surfaces are required for complete inhibition of ice crystal growth. To test this hypothesis, a 7-kDa type III AFP was linked through its N-terminus to thioredoxin (12 kDa) or maltose-binding protein (42 kDa). The resultant 20-kDa and 50-kDa fusion proteins were larger in diameter than free AFP and thus precluded any extensive AFP-AFP contacts on the ice surface. Both fusion proteins were at least as active as free AFP at virtually all concentrations tested. By these criteria, AFPs function independently of each other and do not require specific intermolecular interactions to bind tightly to ice.
ISSN:0006-3495
1542-0086
DOI:10.1016/S0006-3495(98)77862-2