Novel dimeric β-helical model of an ice nucleation protein with bridged active sites

January 2011
BMC Structural Biology;2011, Vol. 11 Issue 1, p36
Academic Journal
The article explains the novel ß-helical fold for the Ice nucleation proteins (INP) produced by the bacterium Pseudomonas borealis. It is mentioned that protein uses internal serine and glutamine ladders for stabilization and is predicted to dimerize through a solvent-exposed tyrosine ladder to make an intimate hydrophobic contact along the dimerization interface. It is found that dimerization increases the ice-active surface area of the protein by doubling its width.


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