Max Perutz (1914-2002)

[Perutz] Sketch by Julia Duax
Early on Wednesday, February 6, Max Perutz died of cancer after a long and productive life. Starting a Ph.D. in 1936 under J.D. Bernal at the Cavendish Laboratory, he applied X-ray crystallography to proteins and in 1953 developed the method of isomorphous replacement using heavy atoms to solve the phase problem. This led to the solution of the first protein structures, those of myoglobin by his colleague John Kendrew and his collaborators, and of haemoglobin by Perutz and his collaborators. For this, Perutz and Kendrew were awarded the 1962 Nobel Prize for Chemistry. With a great deal more work during the 1960’s, Perutz and his colleagues went on to solve the atomic structures of both oxy- and deoxy-haemoglobin which allowed him to propose a stereochemical mechanism for the cooperative binding of oxygen to haemoglobin. Max was the first author of a recent review (Ann. Rev. Biophysics and Biomolecular Structure 1998) of cooperativity in haemoglobin in which he noted that his mechanism still appeared to be correct.

In more recent years, he worked on ligand binding to haemoglobin to help develop a clinically useful drug for increasing oxygen delivery to hypoxic tumours for radiation therapy, and to infarcted tissues. He also developed a strong interest in the structure of the polyglutamine tracts in Huntington’s disease. In his youth, as a sideline, he also worked on glaciers. He studied the transformation of snowflakes that fall on glaciers into the huge single ice crystals that make up its bulk, and the relationship between the mechanical properties of ice measured in the laboratory and the mechanism of glacier flow. He was a prolific and talented writer of popular articles and book reviews, many published in the New York Review of Books. He also wrote a number of books, including 'Is Science Necessary' and 'I wish I’d made you angry earlier' which are collections of essays. 'Science is not a quiet Life' published by World Scientific Publishing is essentially his scientific autobiography.

[Hemaglobin] The porphyrin molecule in hemaglobin. (provided by Anthony Addlagatta)
At the Cavendish Laboratory with the support of Prof. Lawrence Bragg and with his first Ph.D. student, John Kendrew, who joined him in 1945, he built up a group working on the molecular structure of biological systems which grew to four people in 1950 and to about 40 people by 1960. Merging then with other groups from Cambridge and London to create the MRC Laboratory of Molecular Biology on the Hills Road site (now Addenbrooke’s) in 1962, he became Chairman of the new Laboratory until 1979 when he 'retired'. Since then he has worked nearly every day in the Laboratory which has grown to house over 400 people. Over the years, the Laboratory has been a prolific source of discoveries and inventions. In addition to his own research achievements, Max will be remembered for his interest in and warm support of the work of others, and as one of the founders of Molecular Biology

London Times, 2/7/02,