There are nearly 500 variants of Hemoglobin that occur naturally. Most of them exhibit some sort of cooperative binding. In the Cowtown variation, there is a single amino acid mutation that destabilizes the T-state conformation of Hb. What affect would this have on Cowtown's affinity for oxygen? Compare and contrast how the interaction between WT Hb and Mb would differ from the interaction of Hb-Cowtown and Mb. Would this affect the overall amount of oxygen delivered to tissues? In what way?
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