Modified hemoglobin to show cooperativity in oxygen binding

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With the help of sire directed mutagenesis, hemoglobin has been created in which the proximal histidine residues in both alpha and beta subunits have been replaced by glycine. The imidazole ring from the histidine residue can be replaced by adding free imidazole in solution. Would you expect this modified hemoglobin to show cooperativity in oxygen binding? Why or why not?

Reference no: EM1384975

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