myoglobin mī˝əglō´bĭn [key], protein molecule isolated from the cells of vertebrate skeletal muscle that is both a structural and functional relative of hemoglobin, the oxygen-transport protein of the blood of higher animals. Myoglobin, which is composed of a single polypeptide chain of 153 amino acid residues, has the ability to store oxygen by binding it to an iron atom; iron is part of myoglobin's essential chemical composition. The complete amino acid sequence of myoglobin has been determined; it is a relatively small protein with a molecular weight of approximately 17,000 grams per mole. The distribution of myoglobin among the higher animals is a reflection of its physiological function. It is found abundantly in the tissues of diving mammals, e.g., the whale, the seal, and the dolphin. High concentrations of myoglobin in these animals presumably allows them to store sufficient oxygen to remain underwater for long periods. Myoglobin is found abundantly in man only in cardiac muscle, which, by virtue of its essential function, must possess the capacity for continued activity when environmental oxygen concentrations are low. Myoglobin has been investigated intensely and is the first protein molecule to have been completely described in terms of its three-dimensional geometry. This achievement won the British scientist John Kendrew a share in the 1962 Nobel Prize for Chemistry.
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