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Myoglobin is a small oxygen-binding protein found in muscle cells. This nonpolypeptide unit is noncovalently bound to myoglobin and is essential for the biological activity of the protein. Within a hydrophobic cervice formed by the folding of the polypeptide chain is the heme prosthetic group. In fact there are eight alpha-helical secondary structure in myoglobin. X-ray crystallography revealed that the single polypeptide chain of myoglobin consist entirely of alpha-helical secondary structure. Myoglobin is a typical globular protein in that it is a highly folded compact structure with most of the hydrophobic amino acid residues buried in the interior and many of the polar residues on the surface. It was the first protein to have its three-dimensional structure determined by x-ray crystallography by John Kendrew in 1957. Myoglobin is a relatively small protein of mass 17.8kDa made up of 153 amino acids in a single polypeptide chain. 2 Real world examples: How is Myoglobin used?.
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