Max Perutz and John Kendrew | Biography

Max Perutz was born in Vienna, Austria, to parents who were both from prosperous textile manufacturing families. Instead of entering the family business, Perutz became fascinated with chemistry and began studying it in 1932 at the University of Vienna. He joined the Cavendish Laboratory at Cambridge University as a doctoral student in 1936. There, he worked under J. D. Bernal, who was engaged in X-ray analysis of protein.

In 1937 Perutz began studying the structure of hemoglobin (the protein molecule that transports oxygen in the blood) using X-ray diffraction. Perutz was fully supported in his research by the new head of the lab, Sir William Lawrence Bragg, a physicist who had shared the 1915 Nobel Prize in Physics with his father William for being the first to use X-ray scattering to determine atomic structure of a substance. Bragg secured a Rockefeller Foundation grant for Perutz in 1939 after the Nazis in Austria seized the Jewish Perutz family's property. Perutz received his Ph.D. in 1940. Interned during World War II as an enemy, Perutz returned to Cambridge after the war and continued his study of hemoglobin.In 1947 he became head of the newly established Molecular Biology Unit at Cambridge funded by the Medical Research Council. There he was joined by an assistant, the doctoral student John Kendrew.

Kendrew was born in Oxford, England; his father was a well-known climatologist, while his mother was an art historian. He studied chemistry at Trinity College, Cambridge, on a scholarship and graduated in 1939. In his travels for the Air Ministry during World War II, Kendrew met both J. D. Bernal and Linus Pauling, each of whom was interested in using X-ray diffraction to reveal molecular structure. Like Perutz, Kendrew returned to Cambridge at war's end; there, he trained with Perutz in the techniques of X-ray crystallography. After receiving his Ph.D. in 1949, Kendrew remained with Perutz and began a study of the structure of myoglobin through X-ray diffraction.

For many years the two men devoted themselves to parallel painstaking research. While the primary structure of proteins--the amino acid chain--was known, the shape of the chain--the way in which it curved and folded together within the molecule--remained unknown. Proteins being primary elements of life, an understanding of their atomic structure was basic to a deeper understanding of how they function in the body. The only way to elucidate the complex structure of a protein was through X-ray crystallography, a method of bombarding a crystal with X-rays from several different angles, which yields a diffraction picture indicating the arrangement of the atoms within the crystal's molecules. The complexity of the protein molecule made it impossible to get an adequate X-ray diffraction picture--until Perutz in 1953 hit upon the idea of adding a single atom of a heavy metal, such as gold or mercury, which created points of reference that clarified the pattern.

The huge mass of information Perutz and Kendrew accumulated about the 12,000 atoms of hemoglobin and 1,200 atoms of myoglobin could only be processed once high-speed computers became available in the later 1950s. Kendrew, working on the smaller myoglobin molecule, sorted out its atomic arrangement by 1960. Later that year, Perutz established the precise structure of hemoglobin. In 1962 the two men received the Nobel Prize in Chemistry for their years of work, which was seen as paving the way for understanding protein structure and stimulating a general scientific investigation of physical characteristics in terms of molecular structure. A promising offshoot is the possibility of better understanding and treating of protein disorders, such as sickle-cell anemia.