The Crystallographic Community

Nobel Prize in Chemistry 1962

Max Ferdinand Perutz and John Cowdery Kendrew

for their studies of the structures of globular proteins

[MF Perutz]

Max Ferdinand Perutz
Born Vienna, 19 May 1914
Died Cambridge, 6 February 2002

Max Ferdinand Perutz entered Vienna University in 1932, where he, in his own words, "wasted five semesters in an exacting course of inorganic analysis". His curiosity was aroused, however, by organic chemistry, and especially by a course of organic biochemistry, given by F. von Wessely, in which Sir F.G. Hopkins' work at Cambridge was mentioned. It was here that Perutz decided that Cambridge was the place where he wanted to work for his Ph.D. thesis. With financial help from his father he became a research student at the Cavendish Laboratory in Cambridge under J.D. Bernal in September 1936, and he stayed at Cambridge ever since.

After Hitler's invasion in Austria and Czechoslovakia, the family business was expropriated, his parents became refugees, and his own funds were soon exhausted. He was saved by being appointed research assistant to Sir Lawrence Bragg, under a grant from the Rockefeller Foundation, on January 1st, 1939. The grant continued, with various interruptions due to the war, until 1945, when Perutz was given an Imperial Chemical Industries Research Fellowship. In October 1947, he was made head of the newly constituted Medical Research Council Unit for Molecular Biology, with J.C. Kendrew representing its entire staff. He continued holding this post until he was made Chairman of the Medical Research Council Laboratory of Molecular Biology, in March 1962. His collaboration with Sir Lawrence Bragg continued through all these years.

The scientific work of Perutz on the structure of haemoglobin started as a result of a conversation with F. Haurowitz in Prague, in September 1937. G.S. Adair made him the first crystals of horse haemoglobin, and Bernal and I. Fankuchen showed him how to take X-ray pictures and how to interpret them. Early in 1938, Bernal, Fankuchen, and Perutz published a joint paper on X-ray diffraction from crystals of haemoglobin and chymotrypsin. The chymotrypsin crystals were twinned and therefore difficult to work with, and so Perutz continued with haemoglobin. D. Keilin, then Professor of Biology and Parasitology at Cambridge, soon became interested in the work and provided Perutz and his colleagues with the biochemical laboratory facilities which they lacked at the Cavendish. Thus from 1938 until the early fifties the protein chemistry was done at Keilin's Molteno Institute and the X-ray work at the Cavendish, with Perutz busily bridging the gap between biology and physics on his bicycle.

His study of haemoglobin was life long and he helped to design a useful drug to deliver oxygen to tumours and to damaged tissues.

The information on this page is based on content at © The Nobel Foundation. Photograph: A. R. Fersht, 1994

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