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BIOL 2020
K Wheaton

Hemoglobin an allosteric protein 8.1 hemoglobin displays cooperative behaviour  Hemoglobin has a sigmoidal curve 8.2 Myoglobin and hemoglobin bind oxygen in heme groups  Myoglobin, single polypeptide, tertiary structure, composed of alpha helices, globin fold (holds them together)  Heme gives muscle and blood its distinctive red color  consists of 4 pyrrole rings linked by methane bridges  Hemoglobin has yielded the basis for observing the brain in action 8.3 Hemoglobin binds oxygen cooperatively  Hemoglobin  quaternary structure, tetramer, alpha beta dimmers  When going from T to R, the 5 coordination site histidine moves with the iron ion 8.4 An allosteric regulator determines the oxygen affinity of hemoglobin  The interaction is facilitated by ionic bonds between the negative charges on 2, 3- BPG and three positively charged groups of each beta chain  Mutation of sickle cell: reduces the solubility of the deoxygenated but not teh oxygenated form of hemoglobin, therefore sickling results w
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