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Perutz, Max (Ferdinand)

protein haemoglobin ray research

(1914–2002) Austrian–British molecular biologist: showed structure of haemoglobin.

Both sides of Perutz’s family were textile manufacturers. After studying chemistry in Vienna he came to Cambridge in 1936 to work for a PhD in crystallography with J D Bernal (1901–71). The latter had shown in 1934, with , that a wet crystal of a protein (pepsin) would give an X-ray diffraction pattern, thereby implying that it might be possible to use the X-ray method that the had used for inorganic compounds to deduce the structure of proteins. However, Bernal gave Perutz some dull work on minerals and it was 1937 before Perutz secured some crystals of haemoglobin and found them to give excellent X-ray patterns. Haemoglobin is the protein of red blood cells, which carries oxygen to the tissues and CO2 to the lungs.

The invasion of Austria in 1938, and the Second World War (during which he was interned as an alien for a time), diverted Perutz from protein work for a time; but from 1947 he directed a Medical Research Council Unit in Cambridge, consisting at first only of himself and his assistant J C Kendrew (1917–97) who had spent the war in radar, and operational research, with the RAF. In 1953 Perutz showed that the haemoglobin structure could be solved by comparison of two or more X-ray diffraction patterns, one from the pure protein and the others from the same protein with heavy atoms such as mercury attached to it at specific positions. This method led to the solution of the first two protein structures; Perutz and his colleagues solved haemoglobin (relative molecular mass 64 500) and Kendrew and his colleagues solved the related (but simpler) myoglobin from sperm whale muscle. Their methods have been adopted and extended to several hundred other proteins, including enzymes, antibodies and viruses.

The Unit became the Medical Research Council Laboratory of Molecular Biology, chaired for many years by Perutz and a focus of world talent in its field, attracting among others. Perutz and Kendrew shared a Nobel Prize in 1962. Perutz went on to study the structural changes in haemoglobin that occur when it takes up oxygen, and its mutant forms, characteristic of some inherited diseases. Before 1950 Perutz also did research on the crystallography and mechanism of flow of glaciers (which tied in with his passion for skiing and mountaineering). He joined the Order of Merit in 1988 (a UK decoration for those providing valued service to the country, restricted to 24 members).

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