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Model showing structure of haemoglobin molecule

Model showing structure of haemoglobin molecule

P242/0073

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Credit

PROFESSOR MAX PERUTZ, MRC LABORATORY OF MOLECULAR BIOLOGY / SCIENCE PHOTO LIBRARY PROFESSOR MAX PERUTZ, MRC LABORATORY OF MOLECULAR BIOLOGY / SCIENCE PHOTO LIBRARY

Caption

Tertiary, or three-dimensional, conformation of all the atoms making up the haemoglobin molecule. The structure was worked out by Professor Max Perutz using data from X-ray crystallography. Begun in the 1930s, it took 25 years to complete. Haemoglobin is the principal protein present in red blood cells of vertebrate animals. It combines reversibly with molecular oxygen, which it transports from the lungs to the tissues. The molecule consists of four polypeptide chains, each about 145 amino acids in length (the 4 chains are in fact 2 pairs). It contains four atoms of iron, each able to take up one molecule of oxygen.

Release details

Model release not required. Property release not required.

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