Max Perutz: 1914-2002, 1962 Nobel Prize (Chemistry) winner for identifying the structure of Hemoglobin
Dr. Max Perutz will always be associated with hemoglobin. It was Perutz who spent 30 years establishing the structure of this vital protein using X-ray crystallography. He started this task at the time when the laborious calculations had to be done by hand and lived to see the new science of proteomics emerge as a powerful medical tool in the post-genomics era.
Max Ferdinand Perutz was born in Vienna on May 19th, 1914. His parents, Hugo Perutz and Dely Goldschmidt, came from families of textile manufacturers. He was sent to school at the Theresianum, a grammar school derived from an officers' academy created during the days of the empress Maria Theresia, and his parents suggested that he should study law in preparation for entering the family business. However, a good schoolmaster awakened his interest in chemistry, and he had no difficulty in persuading his parents to let him study the subject of his choice.
Perutz read Chemistry at the University of Vienna in 1932-36, grumbling at "wasting five semesters in an exacting course of inorganic analysis
", then went to Cambridge (England) to do his PhD with J.D. Bernal on the crystallographic study of a silicate mineral. In World War II he was, briefly and ridiculously, interned as an enemy alien. Released in 1941 following pressure from Cambridge, Perutz then spent some time on Project Habakkuk, which was later aborted.
In 1944, he returned to his research assistantship with William Lawrence Bragg, then head of the Cavendish Laboratory of Physics at Cambridge. Bragg encouraged Perutz (and later Francis Crick and James Watson) to attempt the impossible - to apply the laborious methods of X-ray crystallography (until then only usable for molecules under a few hundred atoms in size) to proteins and nucleic acids with their tens of thousands or even millions of atoms.
Bragg set Perutz up in the Austin wing of the old Cavendish, as head of the infant Medical Research Council (MRC) Unit for Molecular Biology. Perutz had an initial staff of one - his first PhD student, John Cowdery Kendrew, who set to work on the structure of the protein myoglobin, about a quarter of the size of hemoglobin.
In 1953 came the breakthrough - Perutz discovered how to phase his reflections by using a method that has come to be known as isomorphous replacement - the placement of heavy, intensely scattering atoms at regular positions in the crystal lattice without disturbing its structure. Perutz labelled the active thiol groups (sulphur containing analogue of an alcohol) with mercury and with the additional information this gave him he was able to announce the structure of hemoglobin to 5.5 Angstroms resolution in 1959. Shortly thereafter, Kendrew determined myoglobin to 2.0 Angstroms resolution, and for these heroic achievements both Perutz and Kendrew jointly won the Nobel Prize in 1962.
On Wednesday 6th February, 2002, Max Perutz died of cancer.
Sources:
- The Noble e-museum (www.nobel.se)
- "Chemistry in Britain", May 2002