Max Perutz
Perutz in 1962
Max Ferdinand Perutz

19 May 1914
Died6 February 2002(2002-02-06) (aged 87)
Cambridge, England
Alma mater
Known forHeme-containing proteins
SpouseGisela Clara Peiser (m. 1942; 2 children)
Scientific career
FieldsMolecular biology
InstitutionsUniversity of Cambridge
Laboratory of Molecular Biology
Doctoral advisorJohn Desmond Bernal
Doctoral students

Max Ferdinand Perutz OM CH CBE FRS (19 May 1914 – 6 February 2002)[4] was an Austrian-born British molecular biologist, who shared the 1962 Nobel Prize for Chemistry with John Kendrew, for their studies of the structures of haemoglobin and myoglobin. He went on to win the Royal Medal of the Royal Society in 1971 and the Copley Medal in 1979. At Cambridge he founded and chaired (1962–79) The MRC Laboratory of Molecular Biology (LMB), fourteen of whose scientists have won Nobel Prizes.

Early life and education

Perutz was born in Vienna, the son of Adele "Dely" (Goldschmidt) and Hugo Perutz, a textile manufacturer.[5] His parents were Jewish by ancestry, but had baptised Perutz in the Catholic religion.[6] Although Perutz rejected religion and was an atheist in his later years, he was against offending others for their religious beliefs.[7]

His parents hoped that he would become a lawyer, but he became interested in chemistry while at school. Overcoming his parents' objections he enrolled as a chemistry undergraduate at the University of Vienna and completed his degree in 1936. Made aware by lecturer Fritz von Wessely of the advances being undertaken at the University of Cambridge into biochemistry by a team led by Gowland Hopkins, he asked Professor Mark, who was soon to visit Cambridge, to make inquiries of Hopkins about whether there would be a place for him. Mark forgot, but had visited J.D. Bernal, who was looking for a research student to assist him with studies into X-ray crystallography.[8] Perutz was dismayed as he knew nothing about the subject. Mark countered by saying that he would soon learn. Bernal accepted him as a research student in his crystallography research group at the Cavendish Laboratory. His father had deposited £500 with his London agent to support him. He learnt quickly. Bernal encouraged him to use the X-ray diffraction method to study the structure of proteins. As protein crystals were difficult to obtain, he used horse haemoglobin crystals, and began his doctoral thesis on its structure. Haemoglobin was a subject which was to occupy him for most of his professional career. He completed his Ph.D. under Lawrence Bragg in 1940.[9]

He applied to Kings and St. John's colleges, and became a member of Peterhouse, on the basis that it served the best food. He was elected an Honorary Fellow of Peterhouse 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.

World War II

When Hitler took over Austria in 1938, Perutz's parents managed to escape to Switzerland, but they had lost all of their money. As a result, Perutz lost their financial support. With his ability to ski, experience in mountaineering since childhood and his knowledge of crystals, Perutz was accepted as a member of a three-man team to study the conversion of snow into ice in Swiss glaciers in the summer of 1938. His resulting article for the Proceedings of the Royal Society made him known as an expert on glaciers.[10]

Lawrence Bragg, who was Professor of Experimental Physics at the Cavendish, thought that Perutz's research into haemoglobin had promise and encouraged him to apply for a grant from the Rockefeller Foundation to continue his research. The application was accepted in January 1939 and with the money Perutz was able to bring his parents from Switzerland to England in March 1939.[10]

On the outbreak of World War II, Perutz was rounded up along with other persons of German or Austrian background, and sent to Newfoundland (on orders from Winston Churchill).[11] After being interned for several months he returned to Cambridge. Because of his pre-War research into the changes in the arrangement of the crystals in the layers of a glacier, he was asked for advice on whether if a battalion of commandos were landed in Norway, could they be hidden in shelters under glaciers. His knowledge on the subject of ice then led to him being recruited for Project Habakkuk in 1942. This was a secret project to build an ice platform in the mid-Atlantic, which could be used to refuel aircraft. 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.

Establishment of the Molecular Biology Unit

After the War he returned briefly to glaciology, demonstrating how glaciers flow.[12]

In 1947, Perutz, with the support of Professor Bragg, was successful in obtaining support from the Medical Research Council (MRC) to undertake research into the molecular structure of biological systems. This financial support allowed him to establish the Molecular Biology Unit at the Cavendish Laboratory.[13] Perutz's new unit attracted researchers who realised that the field of molecular biology had great promise; among them were Francis Crick in 1949 and James D. Watson in 1951.

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 haemoglobin, which transports oxygen in the blood.[14] 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.[citation needed]

After 1959, Perutz and his colleagues went on to determine the structure of oxy- and deoxy- haemoglobin 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 haemoglobin 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 anaemia. A further interest was the variation of the haemoglobin molecule from species to species to suit differing habitats and patterns of behaviour. 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".[15]

DNA structure and Rosalind Franklin

Perutz with his wife Gisela at the 1962 Nobel ball

During the early 1950s, while Watson and Crick were trying to determine the structure of deoxyribonucleic acid (DNA), they were given by Perutz an unpublished 1952 progress report for the King's College laboratory of Sir John Randall. This report contained X-ray diffraction images taken by Rosalind Franklin that proved to be crucial in coming to the double-helix structure.

Perutz did this without Franklin's knowledge or permission, and before she had a chance to publish a detailed analysis of the content of her unpublished progress report. Later this action was criticised by Randall and others, in view of the results and the honours resulting from this "gift".

In an effort to clarify this issue, Perutz later published the report, arguing that it included nothing that Franklin had not said in a talk she gave in late 1951, which Watson had attended. Perutz also added that the report was addressed to an MRC committee created to "establish contact between the different groups of people working for the Council". Randall's and Perutz's labs were both funded by the MRC.

The author

In his later years, Perutz was a regular reviewer/essayist for The New York Review of Books on biomedical subjects. Many of these essays are reprinted in his 1998 book, I wish I had made you angry earlier.[16]

In August 1985, The New Yorker published his account of his experiences as an internee during World War II, titled "That Was the War: Enemy Alien".

Perutz won the Lewis Thomas Prize for Writing about Science in 1997.[17]

A collection of Perutz's correspondence was published posthumously in 2009, titled What a Time I Am Having: Selected Letters of Max Perutz.

The scientist-citizen

Perutz attacked the theories of philosophers Sir Karl Popper and Thomas Kuhn and biologist Richard Dawkins in a lecture given at Cambridge on 'Living Molecules' in 1994. He criticised Popper's notion that science progresses through a process of hypothesis formation and refutation, saying that hypotheses are not necessarily the basis of scientific research and, in molecular biology at least, they are not necessarily subject to revision either. For Perutz, Kuhn's notion that science advances in paradigm shifts that are subject to social and cultural pressures is an unfair representation of modern science.

These criticisms extended to scientists who attack religion, in particular to Dawkins. Statements which offend people's religious faith were for Perutz tactless and simply damage the reputation of science, though he did not criticize scientists opposing "demonstrably false" theories such as creationism. He concluded that "even if we do not believe in God, we should try to live as though we did."[18]

Within days of the 11 September attacks in 2001, Perutz wrote to British Prime Minister Tony Blair, appealing to him to not respond with military force: "I am alarmed by the American cries for vengeance and concerned that President Bush's retaliation will lead to the death of thousands more innocent people, driving us into a world of escalating terror and counter-terror. I do hope that you can use your restraining influence to prevent this happening."[19]

Honours and awards

Perutz was elected a Fellow of the Royal Society (FRS) in 1954.[4] In addition to the Nobel Prize for Chemistry in 1962, which he shared with John Kendrew for their respective studies of the structures of haemoglobin and myoglobin,[20] Max Perutz received a number of other important honours: he was appointed a Commander of the Order of the British Empire in 1963, elected to the American Academy of Arts and Sciences that same year,[21] received the Austrian Decoration for Science and Art in 1967, was elected to the American Philosophical Society in 1968,[22] elected to the United States National Academy of Sciences in 1970,[23] received the Royal Medal of the Royal Society in 1971, appointed a Member of the Order of the Companions of Honour in 1975, received the Copley Medal in 1979 and became a Member of the Order of Merit in 1988.

Perutz was made a Member of the German Academy of Sciences Leopoldina in 1964, received an Honorary doctorate from the University of Vienna (1965) and received the Wilhelm Exner Medal in 1967.[24] He was elected to EMBO Membership in 1964.[1]

The European Crystallographic Association established the Max Perutz Prize, named in his honour.[citation needed]


In 1980, Perutz was invited to deliver one of the six lectures for the Royal Institution Christmas Lectures on The Chicken, the Egg and the Molecules.[25]


Personal life

In 1942, Perutz married Gisela Clara Mathilde Peiser (1915–2005), a medical photographer. They had two children, Vivien (b. 1944), an art historian; and Robin (b. 1949), a professor of Chemistry at the University of York. Gisela was a refugee from Germany (she was a Protestant whose own father had been born Jewish).[26]

He died on 6 February 2002 and his ashes were interred with his parents Hugo Perutz and Dely Perutz in the Parish of the Ascension Burial Ground in Cambridge.[27] Gisela died on 17 December 2005 and her ashes were interred in the same grave.[citation needed]


  1. ^ a b Anon (1964). "Max Perutz EMBO member".
  2. ^ Crick, Francis Harry Compton (1954). Polypeptides and proteins : X-ray studies. (PhD thesis). University of Cambridge. OCLC 879394484. EThOS
  3. ^ Moffat, John Keith (1969). X-ray studies of chemically-modified horse haemoglobin. (PhD thesis). University of Cambridge. OCLC 500520334. EThOS
  4. ^ a b Blow, David Mervyn (2004). "Max Ferdinand Perutz OM CH CBE. 19 May 1914 – 6 February 2002: Elected F.R.S. 1954". Biographical Memoirs of Fellows of the Royal Society. 50: 227–256. doi:10.1098/rsbm.2004.0016. JSTOR 4140521. PMID 15768489. S2CID 73986989.
  5. ^ "Max F. Perutz – Facts". Retrieved 9 October 2016.
  6. ^ Dickerson, Richard E. (9 October 2016). "Max Perutz and the secret of life, by Georgina Ferry". Protein Science. 17 (2): 377–379. doi:10.1110/ps.073363908. ISSN 0961-8368. PMC 2222719.
  7. ^ "Perutz rubbishes Popper and Kuhn". TSL EDUCATION LTD. 28 November 1994. Retrieved 19 June 2013. Dr Perutz, said: "It is one thing for scientists to oppose creationism which is demonstrably false but quite another to make pronouncements which offend people's religious faith – that is a form of tactlessness which merely brings science into disrepute. My view of religion and ethics is simple: even if we do not believe in God, we should try to live as though we did."
  8. ^ Medawar & Pyke. Page 108.
  9. ^ "Prof. Dr. Max Ferdinand Perutz > Research Profile". Lindau Nobel Laureate Meetings. 17 June 2015. Retrieved 16 May 2023.
  10. ^ a b Medawar & Pyke. Page 109.
  11. ^ Fersht, Alan R. (2002). "Max Ferdinand Perutz OM FRS". Nature Structural Biology. 9 (4): 245–246. doi:10.1038/nsb0402-245. PMID 11914731.
  12. ^ Gratzer, Walter (5 March 2002). "Max Perutz (1914–2002)". Current Biology. 12 (5): R152–R154. doi:10.1016/S0960-9822(02)00727-3. S2CID 30263181.
  13. ^ Medawar & Pyke. Pages 110 to 111.
  14. ^ Everts, Sarah (2016). "Information Overload". Distillations. 2 (2): 26–33. Retrieved 20 March 2018.
  15. ^ Perutz, Max (1998). "1–11". Science is Not a Quiet Life. World Scientific. ISBN 978-981-4498-51-7.
  16. ^ Max Ferdinand Perutz OM FRS – Nature Structural & Molecular Biology
  17. ^ Lewis Thomas Prize Honors Max Perutz
  18. ^ Patel, Kam Perutz rubbishes Popper and Kuhn, The Times Higher Education Supplement, 25 November 1994
  19. ^ Max Perutz and the Secret of Life, By Georgina Ferry. 352 pp., illustrated. Cold Spring Harbor, NY, Cold Spring Harbor Laboratory Press, 2008 ISBN 978-0-87969-785-3. p. 283 in UK version
  20. ^ Stoddart, Charlotte (1 March 2022). "Structural biology: How proteins got their close-up". Knowable Magazine. doi:10.1146/knowable-022822-1. S2CID 247206999. Retrieved 25 March 2022.
  21. ^ "Max Ferdinand Perutz". American Academy of Arts & Sciences. Retrieved 16 September 2022.
  22. ^ "APS Member History". Retrieved 16 September 2022.
  23. ^ "Max F. Perutz". Retrieved 16 September 2022.
  24. ^ editor, ÖGV. (2015). Wilhelm Exner Medal. Austrian Trade Association. ÖGV. Austria.
  25. ^ "The chicken, the egg and the molecules – Haemoglobin: the breathing molecule (1980)". The Royal Institution of Great Britain. 5 December 1980. Retrieved 17 May 2023.
  26. ^ Max Perutz And The Secret Of Life ISBN 978-1-4464-0265-8
  27. ^ E-mails from Robin Perutz and Vivien Perutz to Martin Packer, August 2012


Academic offices Preceded byAndrew Fielding Huxley Fullerian Professor of Physiology 1973–1979 Succeeded byDavid Chilton Phillips