Myoglobin

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Myoglobin is a single-chain protein of 153 amino acids, containing a heme (iron-containing porphyrin) group in the center. With a molecular weight of 16,700 Daltons, it is the primary oxygen-carrying pigment of muscle tissues. Unlike the blood-borne hemoglobin, to which it is structurally related, this protein does not exhibit cooperative binding of oxygen. Instead, the binding of oxygen by myoglobin is unaffected by the oxygen tension in the surrounding tissue. In 1957, John Kendrew and associates successfully determined the structure of myoglobin by high-resolution X-ray crystallography.

Related Topics:
Single-chain - Protein - Amino acid - Heme - Iron - Porphyrin - Daltons - Oxygen - Pigment - Muscle - Hemoglobin - Cooperative binding - 1957 - John Kendrew - X-ray crystallography

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For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz.

Related Topics:
Nobel Prize in chemistry - Max Perutz

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