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Max Perutz was born in Vienna in 1914. He was educated in the Theresianum (a grammar school originating from an earlier Officers’ academy). His parents suggested that he study law to prepare for entering the family business, but he was allowed to change to chemistry when his interest in this was awakened by a master. In 1932 he entered Vienna University “wasting five semesters in an exacting course of inorganic analysis”. His curiosity was aroused, however, by organic chemistry in which F. G. Hopkins’ work at Cambridge was mentioned and Perutz decided that Cambridge was the place where he wanted to work for his PhD. In 1936, with financial help from his father, he became a research student at the Cavendish Laboratory in a crystallography group directed by J. D. Bernal and has remained in Cambridge ever since. The study of haemoglobin began as a result of a conversation with F. Haurowitz in Prague. Crystals of horse haemoglobin were grown for him by G. S. Adair, and Bernal and I. Fankuchen showed him how to take X-ray pictures and how to interpret them. The three published a joint paper in 1938 on X-ray diffraction from crystals of chymotrypsin and haemoglobin. In 1938, Sir Lawrence Bragg succeeded to Rutherford’s chair at the Cavendish and took over the crystallography group from Bernal, who had moved to London. Perutz was the only remaining member of this group, but Bragg enthusiastically encouraged his X-ray work on haemoglobin. However, internment and subsequent war work prevented much research until after the war. |
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 Complete Molecule of haemoglobin is made up of four subunits, each of which consists of one polypeptide chain and one haem.There are two kinds of subunit, designated alpha (white) and beta (black), which have different sequences of amino acid residues but similar three-dimensional structures. The beta chain also has one short extra helix. The four subunits are arranged at the vertices of a tetrahedron around an axis of two-fold symmetry. Each haem (gray) lies in a separate pocket at the surface of the molecule. |
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In 1953 Perutz showed that the diffracted rays from protein crystals could be phased by comparing the patterns from crystals of the protein with and without heavy atoms attached. The group developed the technique which is now used as a standard method of solving protein structures from crystals, and in 1959 the structure of haemoglobin was solved to 6Å resolution. The Cavendish group was funded as an MRC Unit from 1947 until they moved to the newly built Laboratory of Molecular Biology in 1962. Perutz was the Chairman of the Laboratory until 1979. The work with haemoglobin continued to atomic resolution, and the mechanism by which it ferries oxygen from lungs to tissues and carbon dioxide back to the lungs was established. Recently he has been working on the structural behaviour of the protein modified in Huntington's chorea. Max Perutz died in February 2002 in Cambridge aged 87. |
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