Max Perutz - The Scientist

The Scientist

In 1936, after completing his first university degree at the University of Vienna, Perutz became a research student at the University of Cambridge's Cavendish Laboratory, in a crystallography research group under the direction of J.D. Bernal. He completed his PhD. under William Lawrence Bragg. In Cambridge he started to work on haemoglobin, which was to occupy him for most of his professional career. As a research student Perutz became a member of Peterhouse, where he was elected an Honorary Fellow in 1962. He took a keen interest in the Junior Members, and was a regular and popular speaker at the Kelvin Club, the College's scientific society.

Perutz was exiled from Austria because of his Jewish heritage when Nazi Germany annexed that country prior to World War II. When the war did break out, he was rounded up along with other persons of German or Austrian background, and sent to Canada (on orders from Winston Churchill). During the war he worked on Habakkuk, a secret project to build an ice platform in mid-Atlantic, which could be used to refuel aeroplanes. To that end he investigated the recently invented mixture of ice and woodpulp known as pykrete. He carried out early experiments on pykrete in a secret location underneath Smithfield Meat Market in the City of London. Perutz had been engaged on this project because he had worked on the changes in the arrangement of the crystals in the different layers of a glacier before the War. After the War he returned briefly to glaciology. He demonstrated how glaciers flow.

In 1953 Perutz showed that diffracted X-rays from protein crystals could be phased by comparing the patterns from crystals of the protein with and without heavy atoms attached. In 1959 he employed this method to determine the molecular structure of the protein hemoglobin, which transports oxygen in the blood. This work resulted in his sharing with John Kendrew the 1962 Nobel Prize for Chemistry. Nowadays the molecular structures of several thousand proteins are determined by X-ray crystallography every year.

After 1959, Perutz and his colleagues went on to determine the structure of oxy- and deoxy- hemoglobin at high resolution. As a result, in 1970, he was at last able to suggest how it works as a molecular machine: how it switches between its deoxygenated and its oxygenated states, in turn triggering the uptake of oxygen and then its release to the muscles and other organs. Further work over the next two decades refined and corroborated the proposed mechanism. In addition Perutz studied the structural changes in a number of hemoglobin diseases and how these might affect oxygen binding. He hoped that the molecule could be made to function as a drug receptor and that it would be possible to inhibit or reverse the genetic errors such as those that occur in sickle cell anemia. A further interest was the variation of the hemoglobin molecule from species to species to suit differing habitats and patterns of behavior. In his final years Perutz turned to the study of changes in protein structures implicated in Huntington and other neurodegenerative diseases. He demonstrated that the onset of Huntington disease is related to the number of glutamine repeats as they bind to form what he called a polar zipper.