Explain why the structure of myoglobin makes it function well as
an oxygen-storage protein whereas the...
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Biology
Explain why the structure of myoglobin makes it function well asan oxygen-storage protein whereas the structure of hemoglobin makesit function well as an oxygen-transport protein. Describe brieflythe two principal models for the cooperative binding of ligands toproteins with multiple binding sites.
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a Myoglobin has one heme while haemoglobin has four heme associated with it Heme is a non protein molecule containing protoporphyrin IX that has an chelated iron atom It is present in a small hydrophobic pocket in each polypeptide Myoglobin with its eight alpha helix segments therefore can bind only to one oxygen Haemoglobin has four alpha and beta segments that bind four oxygen Binding of one molecule of oxygen to haemoglobin will increase the affinity of other subunits for three oxygen molecules Release of one oxygen will result in release of other oxygen too This is known as cooperativity of haemoglobin Myoglobin is present in muscle cell where it acts as an oxygen reservoir Myoglobin binds to oxygen that is released by haemoglobin
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