Myoglobin, a hemeprotein present in heart and skeletal muscle, functions both as a reservoir for oxygen, and as an oxygen carrier that increases the rate of transport of oxygen within the muscle cell.
Myoglobin consists of a single polypeptide chain that is structurally similar to the individual subunit polypeptide chains of the hemo globin molecule. This homology makes myoglobin a useful model for interpreting some of the more complex properties of hemoglobin.
Alpha Helical content: Myoglobin is a compact molecule, with approximately 80% of its polypeptide chain folded into eight stretches of alpha helix.
Location of polar and nonpolar amino acid residues: The interior of the myoglobin molecule is composed almost entirely of nonpolar amino acids.
Binding of the heme group: The heme group of myoglobin sits in a crevice in the molecule, which is lined with nonpolar amino acids.
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