Max Perutz

Max Perutz
Name	Max Perutz
Caption	Perutz in 1962
Birth date	19 May 1914
Birth place	Vienna, Austria-Hungary
Death date	6 February 2002
Death place	Cambridge, England
Nationality	Austrian, later British
Fields	Molecular biology, Crystallography
Workplaces	University of Cambridge, Medical Research Council
Alma mater	University of Vienna, University of Cambridge (Peterhouse)
Doctoral advisor	J.D. Bernal
Known for	Determining the three-dimensional structure of haemoglobin
Prizes	Nobel Prize in Chemistry (1962), Royal Medal (1971), Copley Medal (1979)

Max Perutz. He was an Austrian-born British molecular biologist who shared the Nobel Prize in Chemistry in 1962 with John Kendrew for their studies of the structures of globular proteins. Perutz's pioneering work, using X-ray crystallography, revealed the intricate three-dimensional architecture of haemoglobin, the oxygen-carrying protein in red blood cells. His leadership of the Medical Research Council's Laboratory of Molecular Biology in Cambridge helped establish it as a world-renowned centre for structural biology.

Early life and education

Born in Vienna to a prosperous family, he developed an early interest in chemistry and enrolled at the University of Vienna in 1932. Following the rise of the Nazi Party and the Anschluss in 1938, he fled Austria with assistance from William Lawrence Bragg. He continued his studies at the University of Cambridge, joining Peterhouse as a research student under the supervision of J.D. Bernal at the Cavendish Laboratory. His doctoral work involved early attempts to apply X-ray crystallography to biological molecules, focusing initially on chymotrypsin before turning his attention to the formidable challenge of haemoglobin.

Career and research

After World War II, he secured funding from the Medical Research Council to establish a research unit dedicated to the molecular biology of proteins. This unit, initially housed in the Cavendish Laboratory, would later evolve into the famed Laboratory of Molecular Biology at Cambridge. He recruited and mentored a brilliant team, including John Kendrew, Francis Crick, and Sydney Brenner. His own research program was singularly focused on solving the structure of haemoglobin, a project he pursued with remarkable persistence for over two decades, developing crucial techniques like isomorphous replacement and exploiting the properties of heavy atom derivatives.

Haemoglobin structure determination

The breakthrough came in the late 1950s when he successfully applied the method of isomorphous replacement to haemoglobin, using derivatives containing mercury or gold. This allowed him to solve the phase problem in X-ray crystallography. In 1959, his team published the first three-dimensional structure of haemoglobin at low resolution, revealing its complex quaternary structure composed of four polypeptide chains. This monumental achievement explained the protein's cooperative oxygen binding, a fundamental property described by the Hill equation, and provided a direct structural understanding of sickle cell disease as a molecular disease.

Later work and scientific legacy

Following the Nobel Prize in Chemistry, he continued to refine the haemoglobin model and investigate its allosteric mechanisms, influenced by the work of Jacques Monod. He made significant contributions to understanding haemoglobin's role in the Bohr effect and its pathological variants. As a founder and long-time chairman of the Laboratory of Molecular Biology, he fostered an environment where Francis Crick, James Watson, and Frederick Sanger made their historic discoveries. He was also a gifted writer and lecturer, authoring influential essays for publications like the New York Review of Books and books such as I Wish I'd Made You Angry Earlier.

Awards and honours

His numerous accolades include the Nobel Prize in Chemistry in 1962, which he shared with his colleague John Kendrew. He was elected a Fellow of the Royal Society in 1954 and received the Royal Medal in 1971 and the Copley Medal in 1979. He was appointed a Companion of Honour in 1975 and received the Austrian Decoration for Science and Art. Several institutions bear his name, including the Max Perutz Laboratories in Vienna and the European Molecular Biology Laboratory's outstation in Hamburg.

Personal life

He married Gisela Peiser in 1942, and they had two children. He became a naturalised British subject in 1946. An avid mountaineer, he was a member of the Cambridge University Mountaineering Club and participated in an expedition to the Alps that studied the formation of glaciers, leading to a publication in the Proceedings of the Royal Society. He remained scientifically active and engaged in public discourse until his death in Cambridge in 2002.

Category:1914 births Category:2002 deaths Category:Austrian biochemists Category:British Nobel laureates Category:Fellows of the Royal Society