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SOLVED: In human hemoglobin, distal histidine residues were mutated to leucine resulting in a two-fold decrease in oxygen affinity. Do you expect cooperative oxygen binding? Explain your reasoning. b) The wild type hemoglobin has pO2 = 50 Torr. What is the pO2 value for mutated hemoglobin? Draw an oxygen binding curve for wild type hemoglobin with pO2 = 50 Torr and for mutated hemoglobin. The Hill coefficient for both wild type and mutated Hb is 2.8. Use the range of pO2 from 0 Torr to 200 Torr

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