Max Ferdinand Perutz was born in Vienna on May 19th, 1914. Both his parents, Hugo Perutz and Dely Goldschmidt, came from families of textile manufacturers who had made their fortune in the 19th century by the introduction of mechanical spinning and weaving into the Austrian monarchy.

Max Perutz was first educated at the Theresianum, a grammar school derived from an officers’ academy from the days of the Empress Maria Theresia. Many years later he said:“I owe my first step to popularity to scarlet fever which I caught when I was fourteen. To disinfect the classroom, my schoolmates got three days off, for which they thanked me solemnly in a letter signed by the entire class”.

At sixteen, Max won the cup for his school in the skiing competition of the Vienna High Schools, and as a result of that victory his standing at school was transformed.

“For the first time in my life I was treated with a certain degree of respect. From then on our gym teacher always gave me top marks, but they happened to be the only ones in my otherwise mediocre school reports”.

Max aged seven, with his older siblings Franz and Lotte, in Reichenau
 

Pupil at the Theresianum, aged fifteen

Max aged about two, with his Bavarian nanny Cilly Jetzfellner
 

Max was supposed to study law in preparation for entering the family business. However, a good schoolmaster at the Theresianum kindled his interest in chemistry, and he made this the subject of his studies at university.

Although largely disappointed with the way in which the subject was taught, he acquired a special interest in organic biochemistry, having heard about the work of the Nobel Prize winner (and discoverer of vitamins) Sir Gowland Hopkins at Cambridge.

His teacher, Herman Mark, visited Cambridge with plans to pave the way for Perutz to join Hopkins’ group. But Mark met J. D. Bernal, who said that he would take Perutz as his student.

In 1946 Max Perutz was joined in Cambridge by John Kendrew, who set out to work on myoglobin, the much smaller one-chain cousin of haemoglobin. Both spent several years collecting huge amounts of data and using the intensities of the reflections to calculate contour maps (Patterson maps), hoping that these would allow them to determine the haemoglobin structure.

The approach failed. Provoked and inspired by a graduate student (Francis Crick), Perutz decided to attack the so-called phase problem from a different angle.

The Patterson Map

Diffraction photograph of oxyhaemoglobin and the famous haemoglobin model.
 

The breakthrough came in 1953, when Perutz and Kendrew managed to soak a heavy atom (mercury) into their haemoglobin crystal. From the difference produced in the diffraction pattern Perutz was able to deduce the phase of the reflections. To this day, the isomorphous replacement method is still widely used to determine the crystal structure of proteins.

Max Perutz completed the low-resolution 5.5 Å map of haemoglobin in 1959 and a high-resolution 2.8 Å map in 1968. For being the first to successfully determine the structures of complex proteins, Perutz and Kendrew were awarded the Nobel Prize for Chemistry in 1962.

Max Perutz and John C. Kendrew receive the Nobel Prize for Chemistry for their studies of globular proteins.