Nobel Prize Chemistry Blood Myoglobin Autograph Max Perutz Signed Molecular

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Seller: memorabilia111 ✉️ (808) 100%, Location: Ann Arbor, Michigan, US, Ships to: US & many other countries, Item: 176278959896 NOBEL PRIZE CHEMISTRY BLOOD MYOGLOBIN AUTOGRAPH MAX PERUTZ SIGNED MOLECULAR. MAX PERUTZ AUTOGRAPH ON PAPER WITH HIS OFFICIAL ADDRESS AT THE MRC AT CAMBRIDGE. MEASIURES APPROXIMATELY 5 1/2 X 2 3/4 INCHES Max Ferdinand Perutz OM CH CBE FRS 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
Perutz dedicated a large part of his long scientific career to unraveling the molecular structure and function of hemoglobin, the protein of red blood cells. In this work he made pioneering use of x-ray crystallography. He was a co-recipient of the 1962 Nobel Prize for Chemistry and the founder and first chairman of the Medical Research Council Laboratory of Molecular Biology in Cambridge, which produced a string of Nobel Prize winners. Education and Early Career Born into an affluent Viennese family of textile industrialists, Perutz soon resolved not to step into the family business and instead pursue a career in science. He studied chemistry in his hometown. In 1936, after graduation, he joined John Desmond Bernal’s Crystallographic Department at the Cavendish laboratory in Cambridge following an introduction by his teacher Hermann Mark. Perutz had to learn x-ray crystallography from scratch by working on some silicate mineral fragments. Yet from the beginning his aspiration was to work on biological material. A few years before Perutz joined the laboratory, Bernal, together with Dorothy Crowfoot (later Hodgkin), had obtained the first sharp x-ray diffraction images of a protein using crystals in their mother liquid instead of the usual dry crystals. In principle, this observation opened the way to the determination of the atomic structure of proteins. Proteins were considered to hold the key to all life processes, including inheritance; knowing their structure promised to provide clues to their function. Yet by the time Perutz joined the laboratory, Bernal, a key exponent of the scientific Left, was increasingly taken up with political activities connected to the rising threat of a Fascist war. When he moved to London in 1938 to take up a chair at Birkbeck College, Perutz stayed on at the Cavendish. By that time he had settled on a diffraction analysis of hemoglobin as the topic for his PhD thesis. The suggestion had come from the Prague biochemist Felix Haurowitz whom Perutz had asked for advice. Haurowitz had observed that hemoglobin showed a change in crystal form under the microscope when moving from the oxygenated to the deoxygenated form. Gilbert Adair from the Physiology Department in Cambridge supplied the first crystals. Fortunately for Perutz, Bernal’s departure coincided with Lawrence Bragg’s appointment as Ernest Rutherford’s successor to the Cavendish Chair in Cambridge. Bragg became excited at the prospect of extending the method he himself had first applied to propose a structure for common salt some twenty-five years before, to the fantastically complex structure of proteins. When later in 1938 Adolf Hitler annexed Austria and Perutz became an émigré, Bragg obtained a grant from the Rockefeller Foundation that supported Perutz until the end of the war. It also enabled Perutz to have his Jewish parents, Hugo and Adele Perutz, come to Britain and thus escape deportation. Perutz was to dedicate most of his scientific career to the study of the structure and function of the hemoglobin molecule, but he had certainly not anticipated this at the time. The original aims were rather modest, although the hopes to achieve a significant result ran high. To prepare and mount the hemoglobin crystals, determine the dimensions and hydration of the crystals, and study the effects of denaturation was enough to acquire a PhD. Perutz’s dissertation also included the discussion of a two-dimensional vector analysis (also known as Patterson analysis) of a hemoglobin derivative calculated by Dennis Riley of Dorothy Hodgkin’s group in Oxford. Comparison with Hodgkin’s Patterson analysis of insulin led Perutz to confirm that protein molecules were composed of small subunits, arranged in a regular manner. This was a common assumption at the time. It also led crystallographers to believe that the knowledge of the structure of one protein would provide decisive clues for the structure of all proteins. Although these expectations proved wrong, they provided the motivation for researchers including Perutz to approach the problem; without those expectations they might have been discouraged. Internment and Secret War Work Perutz submitted his doctoral dissertation on the structure of hemoglobin in the spring of 1940. A few months later, with mounting fears of a German invasion, he was rounded up with other “enemy aliens.” After prolonged stays in various remote parts of Britain, twelve hundred internees including Perutz were herded on a large troopship that eventually brought them to an internment camp in Canada (while still at sea they learned that another troopship crammed with internees had been sunk by a German U-boat; more than six hundred of the fifteen hundred people on board lost their lives). The humiliating and uncomfortable conditions did not lead to complete despair. With his freshly gained PhD Perutz found himself the doyen of the camp’s scholars and set out to organize a camp university. The staff included several future fellows of the Royal Society, among them the mathematician and cosmologist Hermann Bondi, who was to become chief scientific adviser to the Ministry of Defence, the astronomer Thomas Gold; and Klaus Fuchs, who was to join the Manhattan Project and became an “atom spy,” a role to which he was led not as a German but as a communist. Unknown to Perutz, in the meantime his British colleagues were agitating for his and other internees’ release. He was offered the choice to return to England or take up a professorship at the New School for Social Research in New York, organized as part of a rescue campaign by the Rockefeller Foundation for its grantees. Undeterred by the perils of the transatlantic passage, Perutz opted to return to England. The whole adventure had lasted about eight months. Perutz resumed his research at the Cavendish, but before long was called to participate at a secret wartime project code-named Habakkuk. The plan, conceived by the maverick Geoffrey Pyke, scientific advisor of General Mountbatten, chief of Combined Operations, consisted in building an airplane base made of reinforced ice in the Atlantic. Perutz, who before the war had combined his (lifelong) passion for the mountains and for science by participating in a scientific expedition to the Alps to study the crystalline structure of ice in glaciers, was called to the project as an expert. Working for several months in a cold room at minus 20 degrees Celsius beneath Smithfield Market in London (the rooms were normally used for meat storage), Perutz and his team managed to develop a mixture of ice and wood pulp as strong as concrete; the reinforced ice became known as pykrete. After a successful demonstration of the qualities of pykrete to Franklin Roosevelt and Winston Churchill at their meeting in Quebec in August 1943, Habakkuk gained top priority. The British team was ordered to continue work in Washington. For the overseas mission Perutz was rapidly naturalized and received a British passport. Yet by the time he reached America, Mountbatten had been ordered to Southeast Asia. Having lost its strongest supporter, Habakkuk slid down the priority list and eventually was abandoned. A further reason for the demise of the project was that the rapidly increasing range of aircraft made artificial landing strips in the Atlantic superfluous. In January 1944, Perutz once more returned to his research in the Cavendish. Later he gave a detailed and humorous account of his wartime experience as enemy alien and as scientist on a secret wartime project. “Enemy Alien” first appeared in the New Yorker in August 1985 and established his fame as a writer. It has since been reprinted several times. Structure and Function of Hemoglobin In the last years of the war, Perutz’s work on the structure of hemoglobin was the only piece of pure research still pursued in the Cavendish. Blood and its products, however, were intensively studied in other laboratories because of their relevance to wartime medicine, and Perutz was part of an active network of Cambridge researchers working on different aspects of hemoglobin. The informal group was held together by the physiologist Joseph Barcroft, a pioneer in the field and an inspired teacher. After the war, John Kendrew, a physical chemist who had occupied high offices in operational research during the war and, while on a common mission in Ceylon, had been convinced by Bernal of the promises of protein crystallography, joined Perutz to do a PhD. (Although working closely with Perutz, Kendrew was officially supervised by William T. Taylor, head of the crystallography division at the Cavendish; like most professional crystallographers Taylor regarded protein crystallography as a hopeless undertaking, but still accepted the formal agreement.) Kendrew first embarked on a comparative analysis of fetal and adult hemoglobin, but later switched to the simpler protein myoglobin, the oxygen carrier in muscle. Although Perutz now had a collaborator, his own future was still uncertain. With the end of the war, the Rockefeller grant had run out. Bragg had obtained a two-year Imperial Chemical Industries fellowship for Perutz, but his aim to secure a university post for his protégé looked increasingly bleak. At this critical juncture, the Cambridge parasitologist and biochemist David Keilin, a strong supporter of Perutz’s work, suggested to Bragg to apply to the Medical Research Council (MRC) for funding. The successful application led to the establishment of the MRC Unit for the Study of Molecular Structure of Biological Systems with Perutz as its director. Among the first recruits were Hugh Huxley, Francis Crick, James Watson (who joined as a visitor) and, somewhat later, Sydney Brenner. In 1949 Perutz published a paper in which he proposed the “pill box” or “hat-box” model of hemoglobin. It featured the polypeptide chains running in parallel bundles. Crick, although still a newcomer in the field, forcefully criticized the model and the assumption of a regular arrangement on which it was based. Crick’s attack produced some turmoil, but Perutz recognized the force of his argument. He developed a strong respect for Crick’s sharp judgment and, on several occasions, defended him against the grudge of the Cavendish head who resented his irreverent behavior. The turning point in Perutz’s endeavor to unravel the structure of the complex hemoglobin model came in 1953, when he found a solution to the so-called phase problem. To derive the structure of a molecule from its diffraction pattern both the intensity as well as the phase of each spot were required. Yet while the intensities could be directly measured on the diffraction pictures (up to the mid-1950s this was done by eye), the phases had to be established by other methods. To circumvent the phase problem, Perutz and his colleagues used the Patterson function. It allowed them to calculate the distances between atoms on the basis of the intensities alone, but it left ample space for interpretation regarding the actual position of the atoms in space. The infamous hat-box model still relied on that method. Perutz now managed to attach a heavy atom (mercury) to the hemoglobin molecule. From the difference produced in the diffraction pattern he was able to deduce the phase of the reflections. The method had been known since the 1930s, but it had only been used for small molecules. Although the suggestion to apply the method to proteins dated from the same period, its applicability had not been proved. The problem consisted, firstly, in finding a heavy metal compound that could be attached to a specific site without altering the arrangement of the other atoms in the molecule and, secondly, in estimating with sufficient accuracy the overall changes in intensity produced by the heavy atoms. In Bragg’s judgment, Perutz’s skill in this last respect was “probably unique” at the time (Bragg, 1965, p. 12). To this day, the isomorphous replacement method is considered the key method to determine the crystal structure of proteins. Kendrew, working on the smaller myoglobin molecule, was the first to take full advantage of the new method. In 1958, he presented the first model ever of a globular protein derived by direct structure determination. The model showed the general outline of the molecule; a second model at atomic resolution followed two years later. In the same year Perutz presented the first model of hemoglobin at 5.5 Ångstrøm. Its four subunits proved to be closely related to the myoglobin molecule. The white-and-black disk model built of thermosetting plastic is still widely reproduced. The determination of any of these protein structures could not have been contemplated without the use of ever more powerful electronic computers. Perutz initially distrusted the new calculating devices and resisted resorting to the experimental digital computers developed at the nearby Mathematical Laboratory. Eventually he came around to recognize their usefulness, but he freely admitted that he was always hopeless at computing. He never made use of the machine himself and rather left this part of the work to the younger people in his group. Perutz and Kendrew shared the 1962 Nobel Prize for Chemistry for their work on the structure of proteins. However, for Perutz the challenge posed by hemoglobin continued. He realized that to understand the oxygen-binding function of hemoglobin, including its cooperative effect, he needed an atomic model of both the oxygenated and deoxygenated forms of hemoglobin. This immense task involved measuring several hundred thousand reflections, stretching even the patience of a crystallographer. Perutz and his collaborators completed it in 1970, well thirty-three years after Perutz had taken the first x-ray picture of the molecule. Close examination of the two models led Perutz and his colleagues to propose a cooperative mechanism that saw the different parts of the model clicking back and forth between the two forms. The proposed mechanism included relative movement of the four subunits as well as conformational change of the subunits when oxygen was bound. It beautifully illustrated, and refined, the mechanism of conformational change (or allostery) postulated by the French biochemist Jacques Monod a few years earlier. For his argument, intended to explain regulatory functions in enzymes, Monod had used hemoglobin as a model. As a result, and to Perutz’s delight, hemoglobin was elevated to the status of an “honorary enzyme.” Another important resource for Perutz’s work was the extensive clinical and biochemical knowledge of abnormal hemoglobins gathered by Hermann Lehmann, professor of clinical biochemistry at Cambridge. By building the known amino acid substitutions into the hemoglobin model, clinical symptoms could be explained in molecular terms; at the same time the functional knowledge of the clinic provided decisive clues for deriving the working mechanism of the molecule. The two researchers published a paper (1968) announcing the new field of molecular pathology. Perutz was deeply satisfied that his research was becoming medically important. Although details of Perutz’s proposed mechanism of the hemoglobin model were contested, the model as a whole stood the test of time. Laboratory of Molecular Biology Besides remaining deeply committed to work at the bench, Perutz was an effective institute builder. Throughout the 1950s the MRC Unit at the Cavendish under his direction grew in size and importance. Apart from the protein work that was attracting more researchers, Watson’s arrival in 1951 stirred Crick into a collaboration on the structure of DNA that led to the proposal of the complementary double helical structure of the molecule in 1953. Although only time would confer on it the iconic place it later gained, the DNA model was regarded early on as an important achievement that confirmed the power of structure-function analysis. Watson’s later account of the discovery in the bestselling The Double Helix (1968) put Perutz in the awkward position of appearing as the person who passed on decisive data gained by the London crystallographer Rosalind Franklin contained in a report on her unit’s work to an MRC committee of which he was a member. In a letter to Science Perutz made clear that the report was not confidential and the data had been presented at talks before, although he acknowledged that as a matter of courtesy he should have asked the London unit for permission. Watson responded by apologizing for having misrepresented the incident. The double-helix work gave rise to further research in the Cambridge unit on the mechanism by which DNA is translated into proteins. With the work and the number of researchers it attracted expanding, the unit outgrew its place in the physics laboratory. At this critical juncture Perutz, joining forces with the Cambridge protein biochemist Fred Sanger, applied to the MRC for a new Laboratory of Molecular Biology (known as the LMB). The laboratory opened on the outskirts of Cambridge in 1962. Perutz became its first chair and for seventeen years light-handedly guided the institution, which quickly established itself as a key center of the burgeoning new field of molecular biology. The memorandum written to argue for the new laboratory became the basis for a series of lectures and finally a book on Proteins and Nucleic Acids: Structure and Function (1962), which Perutz liked to regard as the first textbook of the new discipline. Perutz’s approach in leading the laboratory consisted in keeping administration and formal paperwork at a minimum. Asked for the recipe for a successful laboratory such as the LMB, Perutz’s usual answer was that the key lay in picking good people and helping them get what they needed to develop their work and for the rest let them follow their own interests. He also believed that seeing the leading people of a lab doing work at the bench helped boost working morale. Despite disliking committee work, Perutz agreed to act as first chair of the European Molecular Biology Organization, founded in 1963. The main aim of the organization, formed by molecular biologists, was to fund a European fellowship, training, and travel program. However, Perutz remained critical of the plan to found a European molecular biology laboratory, which he thought would become too much a bureaucratic structure and would divert capable people away from existing laboratories. At times Perutz was disappointed that he missed out on a university career, but in later years he increasingly saw the advantages of being able to dedicate all his time to research and to building up the LMB. Active Retirement Perutz retired as chair of the LMB in 1979, but his research work continued. Initially hemoglobin remained at the heart of the problems he tackled. One project concerned the adaptation of hemoglobin in different species. Another, in the end unsuccessful, project aimed at identifying drugs that would improve the solubility of sickle cell hemoglobin. However, the work on ligand binding to hemoglobin led to other clinical investigations. Aged eighty, Perutz for the first time strayed away from hemoglobin and, with several collaborators, started a series of original studies on glutamine repeats in proteins connected to neurodegenerative conditions such as Huntington disease. They showed that proteins carrying the repeats form aggregates that lead to neural cell death. In a paper published shortly before his death, Perutz and his coauthor linked the onset of Huntington’s disease to the length of the glutamine repeat. In his later years Perutz became a regular contributor to the London Review of Books and the New York Review of Books. Scientific biographies fascinated him most. He also wrote autobiographical pieces and personal vignettes of scientists he knew, and engaged with political and moral issues, including the organization and freedom of science, population politics, food production, nuclear energy, and human rights. Many of these topics he addressed in public speeches. In all his writings he emphasized the passionate and heroic aspects of scientific research as well as the humanizing influence of science in society. His essays were collected in two volumes, Is Science Necessary? (1989) and I Wish I’d Made You Angry Earlier(1998), edited by himself. In 1997 he was awarded the Lewis Thomas Prize of the Rockefeller University, which honors the scientist as poet. This was the last in a long series of awards and honors. He was elected a fellow of the Royal Society in 1954 and received the Royal Medal of the Royal Society in 1971 and the Copley Medal of the Royal Society in 1979. He was made a Companion of the British Empire in 1963 and a Companion of Honour in 1975, and was appointed to the Order of Merit in 1988. Among others he was a member of the U.S. National Academy of Sciences and a foreign member of the Pontifical Academy of Sciences. He married Gisela Peiser in 1942 and had a daughter (Vivien) and a son (Robin). He died of cancer. BIBLIOGRAPHY The memoir of the Royal Society (see below) includes a full bibliography. WORKS BY PERUTZ The Crystal Structure of Methaemoglobin. PhD diss., University of Cambridge, 1940. “Recent Developments in the X-Ray Study of Haemoglobin.” In Haemoglobin: A Symposium Based on a Conference Held at Cambridge in June 1948 in Memory of Sir Joseph Barcroft, edited by Francis J. Roughton and John C. Kendrew London: Butterworths Scientific Publications, 1949. With Michael G. Rossmann, Ann F. Cullis, Hilary Muirhead, et al. “Structure of Haemoglobin: A Three-Dimensional Fourier Synthesis at 5.5 Å. Resolution, Obtained by X-Ray Analysis.” Nature 185 (1960): 416–422. Proteins and Nucleic Acids: Structure and Function. Amsterdam: Elsevier, 1962. With Hermann Lehmann. “Molecular Pathology of Human Haemoglobin.” Nature 219 (1968): 402–409. With Maurice H. F. Wilkins and James D. Watson. “DNA Helix.” Science 164 (1969): 1537–1539. “Stereochemistry of Cooperative Effects in Haemoglobin.” Nature 228 (1970): 726–739. Haemoglobin: Mr Max Perutz Interviewed by Mr H. Judson, 13 November 1987. Video interview. Biochemical Society. Available from http://www.filmandsound.ac.uk/. Is Science Necessary? Essays on Science and Scientists. New York: E.P. Dutton, 1989. Includes the autobiographical essay “Enemy Alien.” Science Is No Quiet Life. Videotape of a lecture on his scientific career held at the Kelvin Club in Peterhouse, Cambridge, 12 November 1996. Available from Peterhouse College. Science Is Not a Quiet Life: Unravelling the Atomic Mechanism of Haemoglobin. London: Imperial College Press, 1997. A collection of all Perutz’s major scientific papers, with introduction. I Wish I’d Made You Angry Earlier: Essays on Science, Scientists, and Humanity. Cold Spring Harbor, NY: Cold Spring Harbor Press, 1998. A collection of his major reviews. “Interview with Max Perutz: Discoverer of the Structure of Haemoglobin.” Vega Science Trust interviews with Max Perutz, 2001. Video excerpts available from http://www.vega.org.uk/video/programme/1. With Alan H. Windle. “Cause of Neural Death in Neurodegenerative Disease Attributable to Expansion of Glutamine Repeats.” Nature 412 (2001): 143–144. OTHER SOURCES Blow, David M. “Max Ferdinand Perutz OM CH CBE 19 May 1914–6 February 2002.” Biographical Memoirs of Fellows of the Royal Society 50 (2004): 227–256. Includes a microfiche with a full bibliography of Max Perutz’s publications. A photocopy is available from the Royal Society Library. Bragg, William Lawrence. “First Stages in the X-Ray Analysis of Proteins.” Reports on Progress in Physics 28 (1965): 1–16. Ferry, Georgina. Max Perutz and the Secret of Life. London: Chatto & Windus, 2007. Kendrew, John C., Gerhard Bodo, Howard M. Dintzis, et al. “A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis.” Nature 181 (1958): 662–666. ———, Richard E. Dickerson, Bror E. Strandberg, et al. “Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution.” Nature 185 (1960): 422–427. Olby, Robert. “Perutz, Max Ferdinand (1914–2002).” In Oxford Dictionary of National Biography. Online ed., edited by Lawrence Goldman. Oxford: Oxford University Press, 2006. Available from http://www.oxforddnb.com. Watson, James D. The Double Helix: A Personal Account of the Discovery of the Structure of DNA. New York: Atheneum, 1968. ———, and Francis H. C. Crick. “Molecular Structure of Nucleic Acids: A Structure for Deoxyribose Nucleic Acid.” Nature 171 (1953): 737–738. Soraya de Chadarevian Complete Dictionary of Scientific Biography Max Perutz Views 3,648,174 Updated May 17 2018 Max Perutz Max Perutz (born 1914) pioneered the use of X-ray crystallography to determine the atomic structure of proteins by combining two lines of scientific investigation—the physiology of hemoglobin and the physics of X-ray crystallography. His efforts resulted in his sharing the 1962 Nobel Prize in chemistry with his colleague, biochemist John Cowdery Kendrew. Perutz's work in deciphering the diffraction patterns of protein crystals opened the door for molecular biologists to study the structure and function of enzymes—specific proteins that are the catalysts for biochemical reactions in cells. Known for his impeccable laboratory skills, Perutz produced the best early pictures of protein crystals and used this ability to determine the structure of hemoglobin and the molecular mechanism by which it transports oxygen from the lungs to tissue. A passionate mountaineer and skier, Perutz also applied his expertise in X-ray crystallography to the study of glacier structure and flow. Perutz was born in Vienna, Austria, on May 19, 1914. His parents were Hugo Perutz, a textile manufacturer, and Adele Goldschmidt Perutz. In 1932, Perutz entered the University of Vienna, where he studied organic chemistry. However, he found the university's adherence to classical organic chemistry outdated and backward. By 1926 scientists had determined that enzymes were proteins and had begun to focus on the catalytic effects of enzymes on the chemistry of cells, but Perutz's professors paid scant attention to this new realm of research. In 1934, while searching for a subject for his dissertation, Perutz attended a lecture on organic compounds, including vitamins, under investigation at Cambridge University in England. Anxious to continue his studies in an environment more attuned to recent advances in biochemical research, Perutz decided he wanted to study at Cambridge. His wish to leave Austria and study elsewhere was relatively unique in that day and age, when graduate students seldom had the financial means to study abroad. But Hugo Perutz's textile business provided his son with the initial funds he would need to survive in England on a meager student stipend. In 1936, Perutz landed a position as research student in the Cambridge laboratory of Desmond Bernal, who was pioneering the use of X-ray crystallography in the field of biology. Perutz, however, was disappointed again when he was assigned to research minerals while Bernal closely guarded his crystallography work, discussing it only with a few colleagues and never with students. Despite Perutz's disenchantment with his research assignments and the old, ill-lit, and dingy laboratories he worked in, he received excellent training in the promising field of X-ray crystallography, albeit in the classical mode of mineral crystallography. "Within a few weeks of arriving, " Perutz states in Horace Freeland Judson's Eighth Day of Creation: Makers of the Revolution in Biology, "I realized that Cambridge was where I wanted to spend the rest of my life." During his summer vacation in Vienna in 1937, Perutz met with Felix Haurowitz, a protein specialist married to Perutz's cousin, to seek advice on the future direction of his studies. Haurowitz, who had been studying hemoglobin since the 1920s, convinced Perutz that this was an important protein whose structure needed to be solved because of the integral role it played in physiology. In addition to making blood red, hemoglobin red corpuscles greatly increase the amount of oxygen that blood can transport through the body. Hemoglobin also transports carbon dioxide back to the lungs for disposal. Although new to the physical chemistry and crystallography of hemoglobin, Perutz returned to Cambridge and soon obtained crystals of horse hemoglobin from Gilbert Adair, a leading authority on hemoglobin. Since the main goal of X-ray crystallography at that time was to determine the structure of any protein, regardless of its relative importance in biological activity, Perutz also began to study crystals of the digestive enzyme chymotrypsin. But chymotrypsin crystals proved to be unsuitable for study by X-ray, and Perutz turned his full attention to hemoglobin, which has large crystal structures uniquely suited to X-ray crystallography. At that time, microscopic protein crystal structures were "grown" primarily through placing the proteins in a solution which was then evaporated or cooled below the saturation point. The crystal structures, in effect, are repetitive groups of cells that fit together to fill each space, with the cells representing characteristic groups of the molecules and atoms of the compound crystallized. In the early 1930s, crystallography had been successfully used only in determining the structures of simple crystals of metals, minerals, and salts. However, proteins such as hemoglobin are thousands of times more complex in atomic structure. Physicists William Bragg and Lawrence Bragg, the only father and son to share a Nobel Prize, were pioneers of X-ray crystallography. Focusing on minerals, the Braggs found that as X-rays pass through crystals, they are buffeted by atoms and emerge as groups of weaker beams which, when photographed, produce a discernible pattern of spots. The Braggs discovered that these spots were a manifestation of Fourier synthesis, a method developed in the nineteenth century by French physicist Jean Baptiste Fourier to represent regular signals as a series of sine waves. These waves reflect the distribution of atoms in the crystal. The Braggs successfully determined the amplitude of the waves but were unable to determine their phases, which would provide more detailed information about crystal structure. Although amplitude was sufficient to guide scientists through a series of trial and error experiments for studying simple crystals, proteins were much too complex to be studied with such a haphazard and time consuming approach. Initial attempts at applying X-ray crystallography to the study of proteins failed, and scientists soon began to wonder whether proteins in fact produce X-ray diffraction patterns. However, in 1934, Desmond Bernal and chemist Dorothy Crowfoot Hodgkin at the Cavendish laboratory in Cambridge discovered that by keeping protein crystals wet, specifically with the liquid from which they precipitated, they could be made to give sharply defined X-ray diffraction patterns. Still, it would take twenty-three years before scientists could construct the first model of a protein molecule. Perutz and his family, like many other Europeans in the 1930s, tended to underestimate the seriousness of the growing Nazi regime in Germany. While Perutz himself was safe in England as Germany began to invade its neighboring countries, his parents fled from Vienna to Prague in 1938. That same summer, they again fled to Switzerland from Czechoslovakia, which would soon face the onslaught of the approaching German army. Perutz was shaken by his new classification as a refugee and the clear indication by some people that he might not be welcome in England any longer. He also realized that his father's financial support would certainly dwindle and die out. As a result, in order to vacation in Switzerland in the summer of 1938, Perutz sought a travel grant to apply his expertise in crystallography to the study of glacier structures and flow. His research on glaciers involved crystallographic studies of snow transforming into ice, and he eventually became the first to measure the velocity distributions of a glacier, proving that glaciers flow faster at the surface and slower at the glacier's bed. Finally, in 1940, the same year Perutz received his Ph.D., his work was put to an abrupt halt by the German invasions of Holland and Belgium. Growing increasingly wary of foreigners, the British government arrested all "enemy" aliens, including Perutz. "It was a very nice, very sunny day—a nasty day to be arrested, " Perutz recalls in The Eighth Day of Creation. Transported from camp to camp, Perutz ended up near Quebec, Canada, where many other scientists and intellectuals were imprisoned, including physicists Herman Bondi and Tom Gold. Always active, Perutz began a camp university, employing the resident academicians to teach courses in their specialties. It didn't take the British government long, however, to realize that they were wasting valuable intellectual resources and, by 1941, Perutz followed many of his colleagues back to his home in England and resumed his work with crystals. Perutz, however, wanted to contribute to the war effort. After repeated requests, he was assigned to work on the mysterious and improbable task of developing an aircraft carrier made of ice. The goal of this project was to tow the carrier to the middle of the Atlantic Ocean, where it would serve as a stopping post for aircrafts flying from the United States to Great Britain. Although supported both by then British Prime Minister Winston Churchill and the chief of the British Royal Navy, Lord Louis Mountbatten, the ill-fated project was terminated upon the discovery that the amount of steel needed to construct and support the ice carrier would cost more than constructing it entirely of steel. Perutz married Gisela Clara Peiser on March 28, 1942; the couple later had a son, Robin, and a daughter, Vivian. After the war, in 1945, Perutz was finally able to devote himself entirely to pondering the smeared spots that appeared on the X-ray film of hemoglobin crystals. He returned to Cambridge, and was soon joined by John Kendrew, then a doctoral student, who began to study myoglobin, an enzyme which stores oxygen in muscles. In 1946 Perutz and Kendrew founded the Medical Research Council Unit for Molecular Biology, and Perutz became its director. Many advances in molecular biology would take place there, including the discovery of the structure of deoxyribonucleic acid (DNA). Over the next years, Perutz refined the X-ray crystallography technology and, in 1953, finally solved the difficult phase dilemma with a method known as isomorphous replacement. By adding atoms of mercury—which, like any heavy metal, is an excellent X-ray reflector—to each individual protein molecule, Perutz was able to change the light diffraction pattern. By comparing hemoglobin proteins with mercury attached at different places to hemoglobin without mercury, he found that he had reference points to measure phases of other hemoglobin spots. Although this discovery still required long and assiduous mathematical calculations, the development of computers hastened the process tremendously. By 1957, Kendrew had delineated the first protein structure through crystallography, again working with myoglobin. Perutz followed two years later with a model of hemoglobin. Continuing to work on the model, Perutz and Hilary Muirhead showed that hemoglobin's reaction with oxygen involves a structural change among four subunits of the hemoglobin molecule. Specifically, the four polypeptide chains that form a tetrahedral structure of hemoglobin are rearranged in oxygenated hemoglobin. In addition to its importance to later research on the molecular mechanisms of respiratory transport by hemoglobin, this discovery led scientists to begin research on the structural changes enzymes may undergo in their interactions with various biological processes. In 1962, Perutz and Kendrew were awarded the Nobel Prize in chemistry for their codiscoveries in X-ray crystallography and the structures of hemoglobin and myoglobin, respectively. The same year, Perutz left his post as director of the Unit for Molecular Biology and became chair of its laboratory. The work of Perutz and Kendrew was the basis for growing understanding over the following decades of the mechanism of action of enzymes and other proteins. Specifically, Perutz's discovery of hemoglobin's structure led to a better understanding of hemoglobin's vital attribute of absorbing oxygen where it is plentiful and releasing it where it is scarce. Perutz also conducted research on hemoglobin from the blood of people with sickle-cell anemia and found that a change in the molecule's shape initiates the distortion of venous red cells into a sickle shape that reduces the cells' oxygen-carrying capacity. In The Eighth Day of Creation, Judson remarks that Perutz was known to have a "glass thumb" for the difficult task of growing good crystals, and it was widely acknowledged that for many years Perutz produced the best images of crystal structures. In the book, published in 1979, Perutz's long-time colleague Kendrew remarks that little changed over the years, explaining, "If I had come into the lab thirty years ago, on a Saturday evening, Max would have been in a white coat mounting a crystal—just the same." Although Perutz retired in 1979, he continued to work as a professor for the MRC Lab of Molecular Biology at Cambridge and also served as a patron for the Cambridge University Scientific Society. Further Reading Cambridge University Scientific Society, 1997, "http://cygnus.csi.cam.ac.uk/CambUniv/Societies/cuss/patrons/patrons.htm, " July 22, 1997. Judson, Horace Freeland, The Eighth Day of Creation: Makers of the Revolution in Biology, Simon & Schuster, 1979. "X-rays Mark the Spots, " in The Economist, November 21, 1992, pp. 100-101. □ Encyclopedia of World Biography Perutz, Max (1914-2002) Views 1,867,966 Updated May 29 2018 Perutz, Max (1914-2002) English crystallographer, molecular biologist, and bio-chemist Max Perutz transformed a fascination of geological processes and crystal structure into one of the fundamental techniques upon which modern molecular biology was founded. Ultimately, Perutz pioneered the use of x-ray crystallography to determine the atomic structure of proteins by combining two lines of scientific investigation—the physiology of hemoglobin and the physics of x-ray crystallography. His efforts resulted in his sharing the 1962 Nobel Prize in chemistry with his colleague, biochemist John Kendrew. A passionate mountaineer and skier, Perutz also applied his expertise in x-ray crystallography to the study of glacier structure and flow. Perutz's work in deciphering the diffraction patterns of protein crystals opened the door for molecular biologists to study the structure and function of enzymes—specific proteins that are the catalysts for biochemical reactions in cells. Known for his impeccable laboratory skills, Perutz produced the best early pictures of protein crystals and used this ability to determine the structure of hemoglobin and the molecular mechanism by which it transports oxygen from the lungs to tissue. Perutz was born in Vienna, Austria, on May 19, 1914. His parents were Hugo Perutz, a textile manufacturer, and Adele Goldschmidt Perutz. In 1932, Perutz entered the University of Vienna, where he studied organic chemistry. In 1936, Perutz landed a position as research student in the Cambridge laboratory of Desmond Bernal, who was pioneering the use of x-ray crystallography in the field of biology. Perutz, however, was disappointed again when he was assigned to research minerals while Bernal closely guarded his crystallography work, discussing it only with a few colleagues and never with students. Perutz's received excellent training in the promising field of x-ray crystallography, albeit in the classical mode of mineral crystallography. In the early 1930s, crystallography had been successfully used only in determining the structures of simple crystals of metals , minerals, and salts. However, proteins such as hemoglobin are thousands of times more complex in atomic structure. Physicists William Bragg and Lawrence Bragg, the only father and son to share a Nobel Prize, were pioneers of xray crystallography. Focusing on minerals, the Braggs found that as x rays pass through crystals, they are buffeted by atoms and emerge as groups of weaker beams which, when photographed, produce a discernible pattern of spots. The Braggs discovered that these spots were a manifestation of Fourier synthesis, a method developed in the nineteenth century by French physicist Jean Baptiste Fourier to represent regular signals as a series of sine waves. These waves reflect the distribution of atoms in the crystal. The Braggs successfully determined the amplitude of the waves but were unable to determine their phases, which would provide more detailed information about crystal structure. Although amplitude was sufficient to guide scientists through a series of trial and error experiments for studying simple crystals, proteins were much too complex to be studied with such a haphazard and time consuming approach. Initial attempts at applying x-ray crystallography to the study of proteins failed, and scientists soon began to wonder whether proteins in fact produce x-ray diffraction patterns. However, in 1934, Desmond Bernal and chemist Dorothy Crowfoot Hodgkin at the Cavendish laboratory in Cambridge discovered that by keeping protein crystals wet, specifically with the liquid from which they precipitated, they could be made to give sharply defined x-ray diffraction patterns. Still, it would take 23 years before scientists could construct the first model of a protein molecule. Perutz and his family, like many other Europeans in the 1930s, tended to underestimate the seriousness of the growing Nazi regime in Germany. While Perutz himself was safe in England as Germany began to invade its neighboring countries, his parents fled from Vienna to Prague in 1938. That same summer, they again fled to Switzerland from Czechoslovakia, which would soon face the onslaught of the approaching German army. Perutz was shaken by his new classification as a refugee and the clear indication by some people that he might not be welcome in England any longer. He also realized that his father's financial support would certainly dwindle and die out. As a result, in order to vacation in Switzerland in the summer of 1938, Perutz sought a travel grant to apply his expertise in crystallography to the study of glacier structures and flow. His research on glaciers involved crystallographic studies of snow transforming into ice , and he eventually became the first to measure the velocity distributions of a glacier, proving that glaciers flow faster at the surface and slower at the glacier's bed. Finally, in 1940, the same year Perutz received his Ph.D., his work was put to an abrupt halt by the German invasions of Holland and Belgium. Growing increasingly wary of foreigners, the British government arrested all enemy aliens, including Perutz. Transported from camp to camp, Perutz ended up near Quebec, Canada, where many other scientists and intellectuals were imprisoned, including physicists Herman Bondi and Tom Gold. Always active, Perutz began a camp university, employing the resident academicians to teach courses in their specialties. It didn't take the British government long, however, to realize that they were wasting valuable intellectual resources and, by 1941, Perutz followed many of his colleagues back to his home in England and resumed his work with crystals. Perutz, however, wanted to contribute to the war effort. After repeated requests, he was assigned to work on the mysterious and improbable task of developing an aircraft carrier made of ice. The goal of this project was to tow the carrier to the middle of the Atlantic Ocean, where it would serve as a stopping post for aircrafts flying from the United States to Great Britain. Although supported both by then British Prime Minister Winston Churchill and the chief of the British Royal Navy, Lord Louis Mountbatten, the ill-fated project was terminated upon the discovery that the amount of steel needed to construct and support the ice carrier would cost more than constructing it entirely of steel. Perutz married Gisela Clara Peiser in 1942; the couple later had a son and a daughter. After the war, in 1945, Perutz was finally able to devote himself entirely to the study of hemoglobin crystals. He returned to Cambridge, and was soon joined by John Kendrew. In 1946 Perutz and Kendrew founded the Medical Research Council Unit for Molecular Biology, and Perutz became its director. Many advances in molecular biology would take place there, including the discovery of the structure of deoxyribonucleic acid (DNA). Over the next years, Perutz refined the x-ray crystallography technology. Often bogged down by tedious mathematical calculations, the development of computers hastened the process tremendously. By 1957, Kendrew had delineated the first protein structure through crystallography, again working with myoglobin. In 1962, Perutz and Kendrew were awarded the Nobel Prize in chemistry for their codiscoveries in x-ray crystallography and the structures of hemoglobin and myoglobin, respectively. The same year, Perutz left his post as director of the Unit for Molecular Biology and became chair of its laboratory. Perutz was a Fellow of the Royal Society. He died on February 6, 2002. See also Atomic theory; Crystals and crystallography World of Earth Science Perutz, Max Ferdinand Views 3,336,469 Updated Jun 11 2018 PERUTZ, MAX FERDINAND PERUTZ, MAX FERDINAND (1914–2002), British biochemist and Nobel laureate. Perutz was born in Vienna and went to Cambridge in 1936. In 1947 he became head of a unit of molecular biology, and in 1962 chairman of the Medical Research Council Laboratory of Molecular Biology. In 1937 he started the study of the structure of crystalline proteins by X-ray diffraction. After 30 years this enabled a complete analysis to be made of the positions of all the 2,600 atoms in the myoglobin molecule and the 10,000 atoms in the molecule of hemoglobin, the component of blood which carries oxygen to the body cells. In 1962 Perutz shared the Nobel Prize for chemistry for "research into the structure of globular proteins." Perutz contributed to scientific periodicals, mainly in the above field. He wrote Proteins and Nucleic Acids: Structure and Function (1962). He was elected a fellow of the Royal Society and member of several national academies of science, and was the recipient of other awards. Georgina Ferry has written a superb biography of one of the most influential and likable figures of modern science, Max Perutz of Cambridge University. It may seem strange to some readers to use the term “modern” to describe something that happened half a century ago, but Max was one of a handful of pioneers who began something that nearly all of us benefit from today: Molecular Biology. He first figured out how to solve the crystal structure of a protein and then implemented this with the blood protein hemoglobin. All of us in the field since that time have essentially been developing better and more high-powered ways of doing what Max accomplished in the 1950s with primitive computational facilities that would be scorned today by people with a laptop computer. The bare bones of Perutz's scientific story can be told briefly: In 1936 he came from Vienna to Cambridge to work on his doctorate and became involved in crystalline proteins under J.D. Bernal. After some fantastic wartime adventures (of which more later), he joined a research group in the Cavendish Physics Laboratory headed by William L. Bragg (known later as Sir Lawrence Bragg), the man who essentially “invented” crystal structure analysis and shared a Nobel Prize with his father W.H. Bragg in 1915 for this achievement. Bragg fils had achieved great things in the structures of minerals and inorganic compounds and considered that the next great challenge would be to apply his methods to the structures of proteins and other biological materials. Bragg persuaded the Medical Research Council in 1948 to support Perutz in founding a new laboratory at Cambridge for this work, and Perutz and his graduate student (and later colleague) John Kendrew embarked on their mission. Max continued to work on the four-chain molecule, hemoglobin, while John ultimately chose its one-chain cousin, myoglobin. Progress naturally was easier with the smaller molecule. Kendrew produced a low-resolution 6 Å structure of myoglobin in 1957 and the high-resolution 2 Å structure in 1959. Perutz completed a low-resolution 5.5 Å map of hemoglobin that same year and a high-resolution 2.8 Å map in 1968. In recognition of what they had accomplished, Perutz and Kendrew shared the Nobel Prize in Chemistry in 1962. That same year the Nobel Prize in Biology and Medicine was awarded to Francis Crick and Jim Watson, who in 1953 had solved the structure of DNA in Max's MRC Laboratory. The year 1962 was indeed an annus mirabilis for the Medical Research Council and for Cambridge! This is the bare skeleton of the story. Georgina Ferry's great achievement is to have fleshed out this plot outline into a real drama about real people. In places the book reads like a novel, but its facts are always correct. Max Perutz was not “just” a scientist; he was a fine human being with strong family ties and with interests that ranged far beyond protein structures. In fact, an earlier interest was in the structure and mechanical properties of ice. He was an enthusiastic mountaineer and skier, at home with both granite and glaciers. While I was a postdoctoral with Kendrew in the late 1950s I once asked Max, “Since you like mountains and snow so much, why did you leave Austria to come to Cambridge?” (Topographically, Cambridge has all the character of a pool table.) Max gave a practical answer, “With my working in Cambridge, Gisela (his wife) and I can go back to Switzerland every winter to visit her family and ski to our hearts' content. If I had remained in Vienna, I couldn't have afforded the train fare to Innsbruck!” Max also was a skilled essayist. Two collections, Is Science Necessary? Essays on Science and Scientists (Dutton, 1989) and I Wish I'd Made You Angry Earlier: Essays on Science, Scientists and Humanity (Cold Spring Harbor Laboratory Press, 2003) still make absorbing reading. The title of the latter collection arises from a story that Max tells about his running into the office of Sir Lawrence Bragg and informing him excitedly that he had just obtained experimental proof of the correctness of Linus Pauling's new α-helix model for protein chains. When asked what had impelled him to do the experiments, Max replied “The idea was sparked off by my fury over having missed that beautiful structure myself.” To this, Bragg replied, “I wish I had made you angry earlier!” Ferry presents this incident well, and also tells you why Bragg was so sensitive about not having been the first to arrive at the helical structure of a protein chain. The issue of whether the folded “sausages” of the low-resolution myoglobin map would turn out to be Pauling's α-helices remained. At 2 Å resolution, would they be hollow (the “garden hose” model), and would they show a helical backbone? In 1959, when we completed the high-resolution map of sperm whale myoglobin, John Kendrew celebrated with a garden party at dusk on the lawn of Peterhouse. The electron density sections through the protein were drawn on Plexiglas and stacked atop a light box. I watched Bragg excitedly drag one attendee after another over to the map, point at one particular helix that moved diagonally down the Plexiglas stack, and exclaim excitedly, “Look! Look! It's hollow!” Max's contributions during World War II are curious, and again Ferry tells them well. When Germany annexed Austria in 1938, Austrian citizens in England such as Max Perutz suddenly became “enemy aliens.” Max was questioned and deemed not to be a threat. But 2 years later when Germany invaded Norway and the Netherlands, Britain reacted by rounding up nearly 7000 Austrian and German men over the age of 16, Max among them, and shipped them off to internment camps in Canada! When they heard of this, both Linus Pauling at Caltech and Martin Buerger at MIT quickly offered Max a visiting fellowship, and the Rockefeller Foundation agreed to fund it. But his colleagues in Britain had been raising a storm of protest, and by the middle of January 1941 Max was safely back in Cambridge. Max later wrote up the entire episode entitled “Enemy Alien” in the August 12, 1985, issue of the New Yorker and included a revised and expanded version in both Is Science Necessary? and I Wish I'd Made You Angry Earlier. By an odd twist of fate, Max found himself back in Canada again (and the United States as well), as an expert on the structures and properties of ice, part of a fantastic program to build floating iceberg airfields in the North Atlantic. The organizer of this plan was Geoffrey Pyke, and the iron-hard frozen mixture of sawdust and water was known as “pykrete.” Max was recruited because of his knowledge of ice and glaciers. The project, not surprisingly, came to nothing. One such airfield of reinforced ice would have been 26 times as heavy as the Queen Elizabeth. Again, Ferry tells the story well and illustrates it with contemporary drawings of the proposed frozen aircraft carrier. Max himself wrote everything up after the fact in a 1947 scientific paper for the Journal of Glaciology entitled “A Description of the Iceberg Aircraft Carrier and the Bearing of the Mechanical Properties of Frozen Wood Pulp upon Some Problems of Glacier Flow.” This surely must be Max's least-cited paper, but he includes it in a collection of his scientific papers entitled Science Is Not a Quiet Life: Unraveling the Atomic Mechanism of Haemoglobin (Imperial College Press, 1997). Ferry does a magnificent job of expressing the doubts, difficulties, and uncertainty of Max Perutz's life. Too often “official” biographies have an unrealistically orderly tone: I got up one morning. I had an inspiration. I ran some experiments. I discovered something new and exciting. I published my findings. I received a Nobel Prize. This is far from describing Perutz's life. He began as an upper middle-class child in Vienna, Jewish by ancestry but Catholic by upbringing. He entered the University of Vienna in 1932 at the age of 18, to commence a 7-year program in chemistry that ultimately would conclude with a doctorate. After 3 years he became disillusioned with the intellectual and political atmosphere in Vienna and longed to move to Cambridge to work with the chemist Frederick Hopkins, who had earned a Nobel Prize in physiology in 1929 for his work on vitamins. His mentor in Vienna, Hermann Mark, inexplicably forgot to contact Hopkins to tell him that Max was coming to visit. But while in Cambridge he did meet the physicist and crystallographer J.D. Bernal and was so captivated by the research that he applied and was accepted into Bernal's group in 1936. When Hitler annexed Austria 2 years later, Max's parents and siblings had to flee the country quickly. His brother was a businessman in Prague and happened to have a car with Czech license plates, so parents, brother, and sister grabbed what they could carry and drove north. His brother and sister later elected to flee from Prague to the United States, but his parents went to Zurich, from where they depended on Max to get them into Britain somehow. He succeeded, but the unemployed business executive and the upper-class society wife found little in England to their pleasure. Georgina Ferry relates one aspect of this anti-Nazi exodus that I cannot avoid passing on. It concerns Hermann Mark, Max's mentor. “Mark and his wife also arrived in London via a ‘skiing holiday’ in Switzerland, having converted his wealth into platinum wire which he disguised as coat hangers.” Max's parents, unfortunately, brought no coat hangers with them, and life was difficult at first. Skipping over the Canadian internment and the pykrete mess that have already been described, Max found himself after the war's end still in a junior position at Cambridge with no permanent university appointment and no job security. When John Kendrew came to work with him in 1946, he had to be enrolled officially under W.H. Taylor, the head of the Crystallography Division, because Max had no university status. It was not until the Medical Research Council funded the MRC Laboratory of Molecular Biology in 1948 that Max acquired a permanent Cambridge University appointment. There were no guiding spirits to whisper to the Cambridge administration, “Hire this man. In another 14 years he will win the Nobel Prize!” Max's research also did not go smoothly. His first “pillbox” model for hemoglobin was dead wrong. Bragg, Kendrew, and Perutz failed to beat Pauling to the α-helix, although if they had given their published fourfold helix a little less twist to 3.6 residues per turn, they would have had it. By the mid-1950s they were at an impasse. The best of conventional techniques, Patterson analysis, failed with such a complex molecule. And then Max had a flash of inspiration that led him and John straight to Stockholm. In 1936, the year Max first came to Cambridge, a Glasgow crystallographer named J.M. Robertson had solved the structure of phthalocyanine, using a new method to surmount what was called the “phase problem.” (If you really want a nonmathematical explanation of what this entailed, see my book, Present at the Flood: How Structural Molecular Biology Came About, Sinauer Associates, 2005.) Robertson bound a heavy metal atom to the phthalocyanine molecule, measured the changes in intensities of reflections in the X-ray pattern, and used this information to break the phase paradox. But phthalocyanine has only 40 atoms (not counting hydrogens); hemoglobin has roughly 4800, or 120 times as many. No one believed that binding even the heaviest metal atom to hemoglobin could produce visible changes in X-ray intensities. No one, that is, except Max. With Vernon Ingram's help, he prepared derivatives of hemoglobin in which each molecule had added to it two atoms of either silver or mercury. The consequence was large and measurable changes in X-ray intensities, and this isomorphous replacement process led to a solution of the phase problem and calculation of an electron density map of the protein. Green, Ingram, and Perutz published their paper in 1954: “The Structure of Haemoglobin IV. Sign Determination by the Isomorphous Replacement Method” (Proc. Roy. Soc A 225: 287) and the battle essentially was over. We knew how to solve protein structures. (A footnote to the title page of that paper observes that Perutz was elected a Fellow of the Royal Society in March 1954. Wise move.) Ferry's book is especially valuable in telling us about Max's early years, before he and his laboratory became famous, and in conveying the personal drama behind the bare outline that I have sketched above. Later matters are also covered in Horace Judson's The Eighth Day of Creation (Simon and Schuster, 1979), Soraya de Chadarevian's Designs for Life (Cambridge University Press, 2002), and my own Present at the Flood. Judson covers the entire field of molecular biology, not just structure. Chadarevian focuses primarily on achievements in protein and DNA structure at Cambridge University (admittedly, the most formidable player). Flood is a collection of reprints of key papers, and explanations of them, covering a period roughly from 1933 to 1963. In all of these sources Max Perutz plays a major role. But only in Ferry's book is he placed at the center of attention, and only her book conveys so much of what Max was really like. Unreservedly recommended! 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 Medical Research Council (MRC) Laboratory of Molecular Biology (LMB), fourteen of whose scientists have won Nobel Prizes. Perutz's contributions to molecular biology in Cambridge are documented in The History of the University of Cambridge: Volume 4 (1870 to 1990) published by the Cambridge University Press in 1992. Contents 1 Early life and education 2 Career and research 2.1 World War 2 2.2 Establishment of the Molecular Biology Unit 2.3 DNA structure and Rosalind Franklin 2.4 The author 2.5 The scientist-citizen 2.6 Honours and awards 2.7 Lectures 2.8 Books by Max Perutz 3 Personal life 4 References 5 Bibliography 6 External links Early life and education Perutz was born in Vienna, the son of Adele "Dely" (Goldschmidt) and Hugo Perutz, a textile manufacturer.[5][6] His parents were Jewish by ancestry, but had baptised Perutz in the Catholic religion.[7][8][9] Although Perutz rejected religion and was an atheist in his later years, he was against offending others for their religious beliefs.[10][11] 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 to 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.[12] 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.[citation needed] Career and research Rejected by Kings and St John's colleges he applied to 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 2 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.[13] 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 in March 1939 to England.[13] 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).[14] After being interned for several months he returned to Cambridge. Because of his previous research into the changes in the arrangement of the crystals in the different layers of a glacier before the War 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 in 1942 being recruited for Project Habakkuk. This was a secret project to build an ice platform in 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. He demonstrated how glaciers flow.[15][16][17][18][19] 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.[20] 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.[21] 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. 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.[22] DNA structure and Rosalind Franklin Perutz with his wife Gisela at the 1962 Nobel ball During the early 1950s, while Watson and Crick were frantically 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.[23] In August 1985 The New Yorker also published his account tiled "That Was the War: Enemy Alien" of his experiences as an internee during World War 2. Perutz's flair for writing was a late development. His relative Leo Perutz, a distinguished writer, told Max when he was a boy that he would never be a writer, an unwarranted judgement, as demonstrated by Perutz's remarkable letters written as an undergraduate. They are published in What a Time I Am Having: Selected Letters of Max Perutz. Perutz was delighted to win the Lewis Thomas Prize for Writing about Science in 1997. 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 Richard Dawkins. Statements which offend religious faith were for Perutz tactless and simply damage the reputation of science. They are of quite a different order to criticism of the demonstrably false theory of creationism. He concluded that "even if we do not believe in God, we should try to live as though we did."[24] Within days of the 11 September attacks in 2001, Perutz wrote to British Prime Minister Tony Blair, appealing to him not to 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."[25] 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 studies of the structures of haemoglobin and myoglobin, Max Perutz received a number of other important honours: he was appointed a Commander of the Order of the British Empire in 1963, received the Austrian Decoration for Science and Art in 1967, the Royal Medal of the Royal Society in 1971, appointed a Companion of Honour in 1975, received the Copley Medal in 1979 and 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.[26] He was elected to EMBO Membership in 1964.[1] Lectures In 1980 he was invited to deliver the Royal Institution Christmas Lecture on The Chicken, the Egg and the Molecules. Books by Max Perutz 1962. Proteins and Nucleic Acids: Structure and Function. Amsterdam and London. Elsevier[ISBN missing] 1989. Is Science Necessary? Essays on science and scientists. London. Barrie and Jenkins. ISBN 0-7126-2123-7 1990. Mechanisms of Cooperativity and Allosteric Regulation in Proteins. Cambridge. Cambridge University PressISBN 0-521-38648-9 1992. Protein Structure : New Approaches to Disease and Therapy. New York. Freeman (ISBN 0-7167-7021-0) 1997. Science is Not a Quiet Life : Unravelling the Atomic Mechanism of Haemoglobin. Singapore. World Scientific. ISBN 981-02-3057-5 2002. I Wish I’d Made You Angry Earlier. Cold Spring Harbor, New York. Cold Spring Harbor Laboratory Press. ISBN 978-0-87969-674-0 2009. What a Time I Am Having: Selected Letters of Max Perutz edited by Vivien Perutz. Cold Spring Harbor, New York. Cold Spring Harbor Laboratory Press. ISBN 978-0-87969-864-5 The Nobel Prize (/noʊˈbɛl/ noh-BEL; Swedish: Nobelpriset [nʊˈbɛ̂lːˌpriːsɛt]; Norwegian: Nobelprisen [nʊˈbɛ̀lːˌpriːsn̩]) is five separate prizes that, according to Alfred Nobel's will of 1895, are awarded to ”those who, during the preceding year, have conferred the greatest benefit to humankind.” Nobel Prizes are awarded in the fields of Physics, Chemistry, Physiology or Medicine, Literature, and Peace (Nobel characterized the Peace Prize as "to the person who has done the most or best to advance fellowship among nations, the abolition or reduction of standing armies, and the establishment and promotion of peace congresses").[2] In 1968, Sveriges Riksbank (Sweden's central bank) established the Prize in Economic Sciences in Memory of Alfred Nobel, founder of the Nobel Prize.[2][3][4] Nobel Prizes are widely regarded as the most prestigious awards available in their respective fields.[5][6] Alfred Nobel was a Swedish chemist, engineer, and industrialist most famously known for the invention of dynamite. He died in 1896. In his will, he bequeathed all of his "remaining realisable assets" to be used to establish five prizes which became known as "Nobel Prizes." Nobel Prizes were first awarded in 1901.[2] The prize ceremonies take place annually. Each recipient (known as a "laureate") receives a gold medal, a diploma, and a monetary award. In 2021, the Nobel Prize monetary award is 10,000,000 SEK.[7] A prize may not be shared among more than three individuals, although the Nobel Peace Prize can be awarded to organizations of more than three people.[8] Although Nobel Prizes are not awarded posthumously, if a person is awarded a prize and dies before receiving it, the prize is presented.[9] The Nobel Prizes, beginning in 1901, and the Nobel Memorial Prize in Economic Sciences, beginning in 1969, have been awarded 603 times to 962 people and 25 organizations.[2] Four individuals have received more than one Nobel Prize.[10] Contents 1 History 1.1 Nobel Foundation 1.1.1 Formation of Foundation 1.1.2 Foundation capital and cost 1.2 Inaugural Nobel prizes 1.3 Second World War 1.4 Prize in Economic Sciences 2 Award process 2.1 Nominations 2.2 Selection 2.3 Posthumous nominations 2.4 Recognition time lag 3 Award ceremonies 3.1 Nobel Banquet 3.2 Nobel lecture 4 Prizes 4.1 Medals 4.2 Diplomas 4.3 Award money 5 Controversies and criticisms 5.1 Controversial recipients 5.2 Overlooked achievements 5.3 Emphasis on discoveries over inventions 5.4 Gender disparity 5.5 Status of the Economic Sciences Prize 6 Statistics 7 Specially distinguished laureates 7.1 Multiple laureates 7.2 Family laureates 8 Refusals and constraints 9 Cultural impact 10 See also 11 References 11.1 Sources 11.1.1 Books 12 Further reading 13 External links History A black and white photo of a bearded man in his fifties sitting in a chair. Alfred Nobel had the unpleasant surprise of reading his own obituary, which was titled The merchant of death is dead, in a French newspaper. Alfred Nobel (About this soundlisten (help·info)) was born on 21 October 1833 in Stockholm, Sweden, into a family of engineers.[11] He was a chemist, engineer, and inventor. In 1894, Nobel purchased the Bofors iron and steel mill, which he made into a major armaments manufacturer. Nobel also invented ballistite. This invention was a precursor to many smokeless military explosives, especially the British smokeless powder cordite. As a consequence of his patent claims, Nobel was eventually involved in a patent infringement lawsuit over cordite. Nobel amassed a fortune during his lifetime, with most of his wealth coming from his 355 inventions, of which dynamite is the most famous.[12] In 1888, Nobel was astonished to read his own obituary, titled The merchant of death is dead, in a French newspaper. It was Alfred's brother Ludvig who had died; the obituary was eight years premature. The article disconcerted Nobel and made him apprehensive about how he would be remembered. This inspired him to change his will.[13] On 10 December 1896, Alfred Nobel died in his villa in San Remo, Italy, from a cerebral haemorrhage. He was 63 years old.[14] Nobel wrote several wills during his lifetime. He composed the last over a year before he died, signing it at the Swedish–Norwegian Club in Paris on 27 November 1895.[15][16] To widespread astonishment, Nobel's last will specified that his fortune be used to create a series of prizes for those who confer the "greatest benefit on mankind" in physics, chemistry, physiology or medicine, literature, and peace.[17] Nobel bequeathed 94% of his total assets, 31 million SEK (c. US$186 million, €150 million in 2008), to establish the five Nobel Prizes.[18][19] Owing to skepticism surrounding the will, it was not approved by the Storting in Norway until 26 April 1897.[20] The executors of the will, Ragnar Sohlman and Rudolf Lilljequist, formed the Nobel Foundation to take care of the fortune and to organise the awarding of prizes.[21] Nobel's instructions named a Norwegian Nobel Committee to award the Peace Prize, the members of whom were appointed shortly after the will was approved in April 1897. Soon thereafter, the other prize-awarding organizations were designated. These were Karolinska Institute on 7 June, the Swedish Academy on 9 June, and the Royal Swedish Academy of Sciences on 11 June.[22] The Nobel Foundation reached an agreement on guidelines for how the prizes should be awarded; and, in 1900, the Nobel Foundation's newly created statutes were promulgated by King Oscar II.[17] In 1905, the personal union between Sweden and Norway was dissolved. Nobel Foundation Formation of Foundation Main article: Nobel Foundation A paper with stylish handwriting on it with the title "Testament" Alfred Nobel's will stated that 94% of his total assets should be used to establish the Nobel Prizes. According to his will and testament read in Stockholm on 30 December 1896, a foundation established by Alfred Nobel would reward those who serve humanity. The Nobel Prize was funded by Alfred Nobel's personal fortune. According to the official sources, Alfred Nobel bequeathed 94% of his fortune to the Nobel Foundation that now forms the economic base of the Nobel Prize.[citation needed] The Nobel Foundation was founded as a private organization on 29 June 1900. Its function is to manage the finances and administration of the Nobel Prizes.[23] In accordance with Nobel's will, the primary task of the foundation is to manage the fortune Nobel left. Robert and Ludvig Nobel were involved in the oil business in Azerbaijan, and according to Swedish historian E. Bargengren, who accessed the Nobel family archive, it was this "decision to allow withdrawal of Alfred's money from Baku that became the decisive factor that enabled the Nobel Prizes to be established".[24] Another important task of the Nobel Foundation is to market the prizes internationally and to oversee informal administration related to the prizes. The foundation is not involved in the process of selecting the Nobel laureates.[25][26] In many ways, the Nobel Foundation is similar to an investment company, in that it invests Nobel's money to create a solid funding base for the prizes and the administrative activities. The Nobel Foundation is exempt from all taxes in Sweden (since 1946) and from investment taxes in the United States (since 1953).[27] Since the 1980s, the foundation's investments have become more profitable and as of 31 December 2007, the assets controlled by the Nobel Foundation amounted to 3.628 billion Swedish kronor (c. US$560 million).[28] According to the statutes, the foundation consists of a board of five Swedish or Norwegian citizens, with its seat in Stockholm. The Chairman of the Board is appointed by the Swedish King in Council, with the other four members appointed by the trustees of the prize-awarding institutions. An Executive Director is chosen from among the board members, a deputy director is appointed by the King in Council, and two deputies are appointed by the trustees. However, since 1995, all the members of the board have been chosen by the trustees, and the executive director and the deputy director appointed by the board itself. As well as the board, the Nobel Foundation is made up of the prize-awarding institutions (the Royal Swedish Academy of Sciences, the Nobel Assembly at Karolinska Institute, the Swedish Academy, and the Norwegian Nobel Committee), the trustees of these institutions, and auditors.[28] Foundation capital and cost The capital of the Nobel Foundation today is invested 50% in shares, 20% bonds and 30% other investments (e.g. hedge funds or real estate). The distribution can vary by 10 percent.[29] At the beginning of 2008, 64% of the funds were invested mainly in American and European stocks, 20% in bonds, plus 12% in real estate and hedge funds.[30] In 2011, the total annual cost was approximately 120 million kronor, with 50 million kronor as the prize money. Further costs to pay institutions and persons engaged in giving the prizes were 27.4 million kronor. The events during the Nobel week in Stockholm and Oslo cost 20.2 million kronor. The administration, Nobel symposium, and similar items had costs of 22.4 million kronor. The cost of the Economic Sciences prize of 16.5 Million kronor is paid by the Sveriges Riksbank.[29] Inaugural Nobel prizes A black and white photo of a bearded man in his fifties sitting in a chair. Wilhelm Röntgen received the first Physics Prize for his discovery of X-rays. Once the Nobel Foundation and its guidelines were in place, the Nobel Committees began collecting nominations for the inaugural prizes. Subsequently, they sent a list of preliminary candidates to the prize-awarding institutions. The Nobel Committee's Physics Prize shortlist cited Wilhelm Röntgen's discovery of X-rays and Philipp Lenard's work on cathode rays. The Academy of Sciences selected Röntgen for the prize.[31][32] In the last decades of the 19th century, many chemists had made significant contributions. Thus, with the Chemistry Prize, the academy "was chiefly faced with merely deciding the order in which these scientists should be awarded the prize".[33] The academy received 20 nominations, eleven of them for Jacobus van 't Hoff.[34] Van 't Hoff was awarded the prize for his contributions in chemical thermodynamics.[35][36] The Swedish Academy chose the poet Sully Prudhomme for the first Nobel Prize in Literature. A group including 42 Swedish writers, artists, and literary critics protested against this decision, having expected Leo Tolstoy to be awarded.[37] Some, including Burton Feldman, have criticised this prize because they consider Prudhomme a mediocre poet. Feldman's explanation is that most of the academy members preferred Victorian literature and thus selected a Victorian poet.[38] The first Physiology or Medicine Prize went to the German physiologist and microbiologist Emil von Behring. During the 1890s, von Behring developed an antitoxin to treat diphtheria, which until then was causing thousands of deaths each year.[39][40] The first Nobel Peace Prize went to the Swiss Jean Henri Dunant for his role in founding the International Red Cross Movement and initiating the Geneva Convention, and jointly given to French pacifist Frédéric Passy, founder of the Peace League and active with Dunant in the Alliance for Order and Civilization. Second World War In 1938 and 1939, Adolf Hitler's Third Reich forbade three laureates from Germany (Richard Kuhn, Adolf Friedrich Johann Butenandt, and Gerhard Domagk) from accepting their prizes.[41] They were all later able to receive the diploma and medal.[42] Even though Sweden was officially neutral during the Second World War, the prizes were awarded irregularly. In 1939, the Peace Prize was not awarded. No prize was awarded in any category from 1940 to 1942, due to the occupation of Norway by Germany. In the subsequent year, all prizes were awarded except those for literature and peace.[43] During the occupation of Norway, three members of the Norwegian Nobel Committee fled into exile. The remaining members escaped persecution from the Germans when the Nobel Foundation stated that the committee building in Oslo was Swedish property. Thus it was a safe haven from the German military, which was not at war with Sweden.[44] These members kept the work of the committee going, but did not award any prizes. In 1944, the Nobel Foundation, together with the three members in exile, made sure that nominations were submitted for the Peace Prize and that the prize could be awarded once again.[41] Prize in Economic Sciences Main article: Nobel Memorial Prize in Economic Sciences Map of Nobel laureates by country In 1968, Sweden's central bank Sveriges Riksbank celebrated its 300th anniversary by donating a large sum of money to the Nobel Foundation to be used to set up a prize in honour of Alfred Nobel. The following year, the Sveriges Riksbank Prize in Economic Sciences in Memory of Alfred Nobel was awarded for the first time. The Royal Swedish Academy of Sciences became responsible for selecting laureates. The first laureates for the Economics Prize were Jan Tinbergen and Ragnar Frisch "for having developed and applied dynamic models for the analysis of economic processes".[45][46] The board of the Nobel Foundation decided that after this addition, it would allow no further new prizes.[47] Award process The award process is similar for all of the Nobel Prizes, the main difference being who can make nominations for each of them.[48] File:Announcement Nobelprize Chemistry 2009-3.ogv The announcement of the laureates in Nobel Prize in Chemistry 2009 by Gunnar Öquist, permanent secretary of the Royal Swedish Academy of Sciences File:Announcement Nobelprize Literature 2009-1.ogv 2009 Nobel Prize in Literature announcement by Peter Englund in Swedish, English, and German Nominations Nomination forms are sent by the Nobel Committee to about 3,000 individuals, usually in September the year before the prizes are awarded. These individuals are generally prominent academics working in a relevant area. Regarding the Peace Prize, inquiries are also sent to governments, former Peace Prize laureates, and current or former members of the Norwegian Nobel Committee. The deadline for the return of the nomination forms is 31 January of the year of the award.[48][49] The Nobel Committee nominates about 300 potential laureates from these forms and additional names.[50] The nominees are not publicly named, nor are they told that they are being considered for the prize. All nomination records for a prize are sealed for 50 years from the awarding of the prize.[51][52] Selection The Nobel Committee then prepares a report reflecting the advice of experts in the relevant fields. This, along with the list of preliminary candidates, is submitted to the prize-awarding institutions.[53] There are four awarding institutions for the six prizes awarded: Royal Swedish Academy of Sciences Nobel Assembly at the Karolinska Institute Swedish Academy Norwegian Nobel Committee The institutions meet to choose the laureate or laureates in each field by a majority vote. Their decision, which cannot be appealed, is announced immediately after the vote.[54] A maximum of three laureates and two different works may be selected per award. Except for the Peace Prize, which can be awarded to institutions, the awards can only be given to individuals.[55] Posthumous nominations Although posthumous nominations are not presently permitted, individuals who died in the months between their nomination and the decision of the prize committee were originally eligible to receive the prize. This has occurred twice: the 1931 Literature Prize awarded to Erik Axel Karlfeldt, and the 1961 Peace Prize awarded to UN Secretary General Dag Hammarskjöld. Since 1974, laureates must be thought alive at the time of the October announcement. There has been one laureate, William Vickrey, who in 1996 died after the prize (in Economics) was announced but before it could be presented.[56] On 3 October 2011, the laureates for the Nobel Prize in Physiology or Medicine were announced; however, the committee was not aware that one of the laureates, Ralph M. Steinman, had died three days earlier. The committee was debating about Steinman's prize, since the rule is that the prize is not awarded posthumously.[9] The committee later decided that as the decision to award Steinman the prize "was made in good faith", it would remain unchanged.[57] Recognition time lag Nobel's will provided for prizes to be awarded in recognition of discoveries made "during the preceding year". Early on, the awards usually recognised recent discoveries.[58] However, some of those early discoveries were later discredited. For example, Johannes Fibiger was awarded the 1926 Prize in Physiology or Medicine for his purported discovery of a parasite that caused cancer.[59] To avoid repeating this embarrassment, the awards increasingly recognised scientific discoveries that had withstood the test of time.[60][61][62] According to Ralf Pettersson, former chairman of the Nobel Prize Committee for Physiology or Medicine, "the criterion 'the previous year' is interpreted by the Nobel Assembly as the year when the full impact of the discovery has become evident."[61] A room with pictures on the walls. In the middle of the room there is a wooden table with chairs around it. The committee room of the Norwegian Nobel Committee The interval between the award and the accomplishment it recognises varies from discipline to discipline. The Literature Prize is typically awarded to recognise a cumulative lifetime body of work rather than a single achievement.[63][64] The Peace Prize can also be awarded for a lifetime body of work. For example, 2008 laureate Martti Ahtisaari was awarded for his work to resolve international conflicts.[65][66] However, they can also be awarded for specific recent events.[67] For instance, Kofi Annan was awarded the 2001 Peace Prize just four years after becoming the Secretary-General of the United Nations.[68] Similarly Yasser Arafat, Yitzhak Rabin, and Shimon Peres received the 1994 award, about a year after they successfully concluded the Oslo Accords.[69] Awards for physics, chemistry, and medicine are typically awarded once the achievement has been widely accepted. Sometimes, this takes decades – for example, Subrahmanyan Chandrasekhar shared the 1983 Physics Prize for his 1930s work on stellar structure and evolution.[70][71] Not all scientists live long enough for their work to be recognised. Some discoveries can never be considered for a prize if their impact is realised after the discoverers have died.[72][73][74] Award ceremonies Two men standing on a stage. The man to the left is clapping his hands and looking towards the other man. The second man is smiling and showing two items to an audience not seen on the image. The items are a diploma which includes a painting and a box containing a gold medal. Behind them is a blue pillar clad in flowers. A man in his fifties standing behind a desk with computers on it. On the desk is a sign reading "Kungl. Vetensk. Akad. Sigil". Left: Barack Obama after receiving the Nobel Peace Prize in Oslo City Hall from the hands of Norwegian Nobel Committee Chairman Thorbjørn Jagland in 2009; Right: Giovanni Jona-Lasinio presenting Yoichiro Nambu's Nobel Lecture at Aula Magna, Stockholm in 2008 Except for the Peace Prize, the Nobel Prizes are presented in Stockholm, Sweden, at the annual Prize Award Ceremony on 10 December, the anniversary of Nobel's death. The recipients' lectures are normally held in the days prior to the award ceremony. The Peace Prize and its recipients' lectures are presented at the annual Prize Award Ceremony in Oslo, Norway, usually on 10 December. The award ceremonies and the associated banquets are typically major international events.[75][76] The Prizes awarded in Sweden's ceremonies' are held at the Stockholm Concert Hall, with the Nobel banquet following immediately at Stockholm City Hall. The Nobel Peace Prize ceremony has been held at the Norwegian Nobel Institute (1905–1946), at the auditorium of the University of Oslo (1947–1989), and at Oslo City Hall (1990–present).[77] The highlight of the Nobel Prize Award Ceremony in Stockholm occurs when each Nobel laureate steps forward to receive the prize from the hands of the King of Sweden. In Oslo, the chairman of the Norwegian Nobel Committee presents the Nobel Peace Prize in the presence of the King of Norway and the Norwegian royal family.[76][78] At first, King Oscar II did not approve of awarding grand prizes to foreigners. It is said[by whom?] that he changed his mind once his attention had been drawn to the publicity value of the prizes for Sweden.[79] Nobel Banquet Main article: Nobel Banquet A set table with a white table cloth. There are many plates and glasses plus a menu visible on the table. Table at the 2005 Nobel Banquet in Stockholm After the award ceremony in Sweden, a banquet is held in the Blue Hall at the Stockholm City Hall, which is attended by the Swedish Royal Family and around 1,300 guests. The Nobel Peace Prize banquet is held in Norway at the Oslo Grand Hotel after the award ceremony. Apart from the laureate, guests include the president of the Storting, on occasion the Swedish prime minister, and, since 2006, the King and Queen of Norway. In total, about 250 guests attend. Nobel lecture According to the statutes of the Nobel Foundation, each laureate is required to give a public lecture on a subject related to the topic of their prize.[80] The Nobel lecture as a rhetorical genre took decades to reach its current format.[81] These lectures normally occur during Nobel Week (the week leading up to the award ceremony and banquet, which begins with the laureates arriving in Stockholm and normally ends with the Nobel banquet), but this is not mandatory. The laureate is only obliged to give the lecture within six months of receiving the prize, but some have happened even later. For example, US President Theodore Roosevelt received the Peace Prize in 1906 but gave his lecture in 1910, after his term in office.[82] The lectures are organized by the same association which selected the laureates.[83] Prizes Medals The Nobel Foundation announced on 30 May 2012 that it had awarded the contract for the production of the five (Swedish) Nobel Prize medals to Svenska Medalj AB. Between 1902 and 2010, the Nobel Prize medals were minted by Myntverket (the Swedish Mint), Sweden's oldest company, which ceased operations in 2011 after 107 years. In 2011, the Mint of Norway, located in Kongsberg, made the medals. The Nobel Prize medals are registered trademarks of the Nobel Foundation.[84] Each medal features an image of Alfred Nobel in left profile on the obverse. The medals for physics, chemistry, physiology or medicine, and literature have identical obverses, showing the image of Alfred Nobel and the years of his birth and death. Nobel's portrait also appears on the obverse of the Peace Prize medal and the medal for the Economics Prize, but with a slightly different design. For instance, the laureate's name is engraved on the rim of the Economics medal.[85] The image on the reverse of a medal varies according to the institution awarding the prize. The reverse sides of the medals for chemistry and physics share the same design.[86] A heavily decorated paper with the name "Fritz Haber" on it. Laureates receive a heavily decorated diploma together with a gold medal and the prize money. Here Fritz Haber's diploma is shown, which he received for the development of a method to synthesise ammonia. All medals made before 1980 were struck in 23 carat gold. Since then, they have been struck in 18 carat green gold plated with 24 carat gold. The weight of each medal varies with the value of gold, but averages about 175 grams (0.386 lb) for each medal. The diameter is 66 millimetres (2.6 in) and the thickness varies between 5.2 millimetres (0.20 in) and 2.4 millimetres (0.094 in).[87] Because of the high value of their gold content and tendency to be on public display, Nobel medals are subject to medal theft.[88][89][90] During World War II, the medals of German scientists Max von Laue and James Franck were sent to Copenhagen for safekeeping. When Germany invaded Denmark, Hungarian chemist (and Nobel laureate himself) George de Hevesy dissolved them in aqua regia (nitro-hydrochloric acid), to prevent confiscation by Nazi Germany and to prevent legal problems for the holders. After the war, the gold was recovered from solution, and the medals re-cast.[91] Diplomas Nobel laureates receive a diploma directly from the hands of the King of Sweden, or in the case of the peace prize, the chairman of the Norwegian Nobel Committee. Each diploma is uniquely designed by the prize-awarding institutions for the laureates that receive them.[85] The diploma contains a picture and text in Swedish which states the name of the laureate and normally a citation of why they received the prize. None of the Nobel Peace Prize laureates has ever had a citation on their diplomas.[92][93] Award money The laureates are given a sum of money when they receive their prizes, in the form of a document confirming the amount awarded.[85] The amount of prize money depends upon how much money the Nobel Foundation can award each year. The purse has increased since the 1980s, when the prize money was 880,000 SEK per prize (c. 2.6 million SEK altogether, US$350,000 today). In 2009, the monetary award was 10 million SEK (US$1.4 million).[94][95] In June 2012, it was lowered to 8 million SEK.[96] If two laureates share the prize in a category, the award grant is divided equally between the recipients. If there are three, the awarding committee has the option of dividing the grant equally, or awarding one-half to one recipient and one-quarter to each of the others.[97][98][99] It is common for recipients to donate prize money to benefit scientific, cultural, or humanitarian causes.[100][101] Controversies and criticisms Main article: Nobel Prize controversies Controversial recipients When it was announced that Henry Kissinger was to be awarded the Peace Prize, two of the Norwegian Nobel Committee members resigned in protest. Among other criticisms, the Nobel Committees have been accused of having a political agenda, and of omitting more deserving candidates. They have also been accused of Eurocentrism, especially for the Literature Prize.[102][103][104] Peace Prize Among the most criticised Nobel Peace Prizes was the one awarded to Henry Kissinger and Lê Đức Thọ. This led to the resignation of two Norwegian Nobel Committee members.[105] Kissinger and Thọ were awarded the prize for negotiating a ceasefire between North Vietnam and the United States in January 1973. However, when the award was announced, both sides were still engaging in hostilities.[106] Critics sympathetic to the North announced that Kissinger was not a peace-maker but the opposite, responsible for widening the war. Those hostile to the North and what they considered its deceptive practices during negotiations were deprived of a chance to criticise Lê Đức Thọ, as he declined the award.[51][107] The satirist and musician Tom Lehrer has remarked that "political satire became obsolete when Henry Kissinger was awarded the Nobel Peace Prize."[108] Yasser Arafat, Shimon Peres, and Yitzhak Rabin received the Peace Prize in 1994 for their efforts in making peace between Israel and Palestine.[51][109] Immediately after the award was announced, one of the five Norwegian Nobel Committee members denounced Arafat as a terrorist and resigned.[110] Additional misgivings about Arafat were widely expressed in various newspapers.[111] Another controversial Peace Prize was that awarded to Barack Obama in 2009.[112] Nominations had closed only eleven days after Obama took office as President of the United States, but the actual evaluation occurred over the next eight months.[113] Obama himself stated that he did not feel deserving of the award, or worthy of the company in which it would place him.[114][115] Past Peace Prize laureates were divided, some saying that Obama deserved the award, and others saying he had not secured the achievements to yet merit such an accolade. Obama's award, along with the previous Peace Prizes for Jimmy Carter and Al Gore, also prompted accusations of a liberal bias.[116] Literature Prize The award of the 2004 Literature Prize to Elfriede Jelinek drew a protest from a member of the Swedish Academy, Knut Ahnlund. Ahnlund resigned, alleging that the selection of Jelinek had caused "irreparable damage to all progressive forces, it has also confused the general view of literature as an art". He alleged that Jelinek's works were "a mass of text shovelled together without artistic structure".[117][118] The 2009 Literature Prize to Herta Müller also generated criticism. According to The Washington Post, many US literary critics and professors were ignorant of her work.[119] This made those critics feel the prizes were too Eurocentric.[120] Science prizes In 1949, the neurologist António Egas Moniz received the Physiology or Medicine Prize for his development of the prefrontal leucotomy. The previous year, Dr. Walter Freeman had developed a version of the procedure which was faster and easier to carry out. Due in part to the publicity surrounding the original procedure, Freeman's procedure was prescribed without due consideration or regard for modern medical ethics. Endorsed by such influential publications as The New England Journal of Medicine, leucotomy or "lobotomy" became so popular that about 5,000 lobotomies were performed in the United States in the three years immediately following Moniz's receipt of the Prize.[121][122] Overlooked achievements Mahatma Gandhi, although nominated five times, was never awarded a Nobel Peace Prize Although Mahatma Gandhi, an icon of nonviolence in the 20th century, was nominated for the Nobel Peace Prize five times, in 1937, 1938, 1939, 1947, and a few days before he was assassinated on 30 January 1948, he was never awarded the prize.[123][124][125] In 1948, the year of Gandhi's death, the Norwegian Nobel Committee decided to make no award that year on the grounds that "there was no suitable living candidate".[123][126] In 1989, this omission was publicly regretted, when the 14th Dalai Lama was awarded the Peace Prize, the chairman of the committee said that it was "in part a tribute to the memory of Mahatma Gandhi".[127] Geir Lundestad, 2006 Secretary of Norwegian Nobel Committee, said, "The greatest omission in our 106 year history is undoubtedly that Mahatma Gandhi never received the Nobel Peace Prize. Gandhi could do without the Nobel Peace Prize. Whether Nobel committee can do without Gandhi is the question."[128] Other high-profile individuals with widely recognised contributions to peace have been overlooked. An article in Foreign Policy magazine identified seven people who "never won the prize, but should have". The list consisted of Gandhi, Eleanor Roosevelt, Václav Havel, Ken Saro-Wiwa, Sari Nusseibeh, Corazon Aquino, and Liu Xiaobo.[125] Liu Xiaobo would go on to win the 2010 Nobel Peace Prize while imprisoned. In 1965, UN Secretary General U Thant was informed by the Norwegian Permanent Representative to the UN that he would be awarded that year's prize and asked whether or not he would accept. He consulted staff and later replied that he would. At the same time, Chairman Gunnar Jahn of the Nobel Peace prize committee, lobbied heavily against giving U Thant the prize and the prize was at the last minute awarded to UNICEF. The rest of the committee all wanted the prize to go to U Thant, for his work in defusing the Cuban Missile Crisis, ending the war in the Congo, and his ongoing work to mediate an end to the Vietnam War. The disagreement lasted three years and in 1966 and 1967 no prize was given, with Gunnar Jahn effectively vetoing an award to U Thant.[129][130] James Joyce, one of the controversial omissions of the Literature Prize The Literature Prize also has controversial omissions. Adam Kirsch has suggested that many notable writers have missed out on the award for political or extra-literary reasons. The heavy focus on European and Swedish authors has been a subject of criticism.[131][132] The Eurocentric nature of the award was acknowledged by Peter Englund, the 2009 Permanent Secretary of the Swedish Academy, as a problem with the award and was attributed to the tendency for the academy to relate more to European authors.[133] This tendency towards European authors still leaves many European writers on a list of notable writers that have been overlooked for the Literature Prize, including Leo Tolstoy, Anton Chekhov, J. R. R. Tolkien, Émile Zola, Marcel Proust, Vladimir Nabokov, James Joyce, August Strindberg, Simon Vestdijk, Karel Čapek, the New World's Jorge Luis Borges, Ezra Pound, John Updike, Arthur Miller, Mark Twain, and Africa's Chinua Achebe.[134] Candidates can receive multiple nominations the same year. Gaston Ramon received a total of 155[135] nominations in physiology or medicine from 1930 to 1953, the last year with public nomination data for that award as of 2016. He died in 1963 without being awarded. Pierre Paul Émile Roux received 115[136] nominations in physiology or medicine, and Arnold Sommerfeld received 84[137] in physics. These are the three most nominated scientists without awards in the data published as of 2016.[138] Otto Stern received 79[139] nominations in physics 1925–1943 before being awarded in 1943.[140] The strict rule against awarding a prize to more than three people is also controversial.[141] When a prize is awarded to recognise an achievement by a team of more than three collaborators, one or more will miss out. For example, in 2002, the prize was awarded to Koichi Tanaka and John Fenn for the development of mass spectrometry in protein chemistry, an award that did not recognise the achievements of Franz Hillenkamp and Michael Karas of the Institute for Physical and Theoretical Chemistry at the University of Frankfurt.[142][143] According to one of the nominees for the prize in physics, the three person limit deprived him and two other members of his team of the honor in 2013: the team of Carl Hagen, Gerald Guralnik, and Tom Kibble published a paper in 1964 that gave answers to how the cosmos began, but did not share the 2013 Physics Prize awarded to Peter Higgs and François Englert, who had also published papers in 1964 concerning the subject. All five physicists arrived at the same conclusion, albeit from different angles. Hagen contends that an equitable solution is to either abandon the three limit restriction, or expand the time period of recognition for a given achievement to two years.[144] Similarly, the prohibition of posthumous awards fails to recognise achievements by an individual or collaborator who dies before the prize is awarded. The Economics Prize was not awarded to Fischer Black, who died in 1995, when his co-author Myron Scholes received the honor in 1997 for their landmark work on option pricing along with Robert C. Merton, another pioneer in the development of valuation of stock options. In the announcement of the award that year, the Nobel committee prominently mentioned Black's key role. Political subterfuge may also deny proper recognition. Lise Meitner and Fritz Strassmann, who co-discovered nuclear fission along with Otto Hahn, may have been denied a share of Hahn's 1944 Nobel Chemistry Award due to having fled Germany when the Nazis came to power.[145] The Meitner and Strassmann roles in the research was not fully recognised until years later, when they joined Hahn in receiving the 1966 Enrico Fermi Award. Emphasis on discoveries over inventions Alfred Nobel left his fortune to finance annual prizes to be awarded "to those who, during the preceding year, shall have conferred the greatest benefit on mankind".[146] He stated that the Nobel Prizes in Physics should be given "to the person who shall have made the most important 'discovery' or 'invention' within the field of physics". Nobel did not emphasise discoveries, but they have historically been held in higher respect by the Nobel Prize Committee than inventions: 77% of the Physics Prizes have been given to discoveries, compared with only 23% to inventions. Christoph Bartneck and Matthias Rauterberg, in papers published in Nature and Technoetic Arts, have argued this emphasis on discoveries has moved the Nobel Prize away from its original intention of rewarding the greatest contribution to society.[147][148] Gender disparity There have been a total of 57 women Nobel laureates compared to 873 male laureates. Most female laureates received them in the peace and literature categories. Marie Curie was the first female to receive the Nobel Prize in 1903 and the only woman to receive it twice. See also: List of female Nobel laureates In terms of the most prestigious awards in STEM fields, only a small proportion have been awarded to women. Out of 210 laureates in Physics, 181 in Chemistry and 216 in Medicine between 1901 and 2018, there were only three female laureates in physics, five in chemistry and 12 in medicine.[149][150][151][152] Factors proposed to contribute to the discrepancy between this and the roughly equal human sex ratio include biased nominations, fewer women than men being active in the relevant fields, Nobel Prizes typically being awarded decades after the research was done (reflecting a time when gender bias in the relevant fields was greater), a greater delay in awarding Nobel Prizes for women's achievements making longevity a more important factor for women (one cannot be nominated to the Nobel Prize posthumously), and a tendency to omit women from jointly awarded Nobel Prizes.[153][154][155][156][157][158] Despite these factors, Marie Curie is to date the only person awarded Nobel Prizes in two different sciences (Physics in 1903, Chemistry in 1911); she is one of only three people who have received two Nobel Prizes in sciences (see Multiple laureates below). Status of the Economic Sciences Prize Peter Nobel describes the "Bank of Sweden Prize in Economic Sciences in Memory of Alfred Nobel" as a "false Nobel prize". Mr Nobel says that this prize dishonours his relative Alfred Nobel, after whom the prize is named. Peter considers "economics" to be a pseudoscience.[159][160] Statistics Youngest person to receive a Nobel Prize: Malala Yousafzai; at the age of 17, received Nobel Peace Prize (2014). Oldest person to receive a Nobel Prize: John B. Goodenough; at the age of 97, received Nobel Prize in Chemistry (2019). Only person to receive more than one unshared Nobel Prize: Linus Pauling; received the prize twice. Nobel Prize in Chemistry (1954) and Nobel Peace Prize (1962). Laureates who have received Multiple Nobel Prizes: (by date of second Prize) Marie Curie; received the prize twice. Nobel Prize in Physics (1903) and Nobel Prize in Chemistry (1911). International Committee of the Red Cross; received the prize three times. Nobel Peace Prize (1917, 1944, 1963). Linus Pauling; received the prize twice. Nobel Prize in Chemistry (1954) and Nobel Peace Prize (1962). John Bardeen; received the prize twice. Nobel Prize in Physics (1956, 1972). Frederick Sanger; received the prize twice. Nobel Prize in Chemistry (1958, 1980). United Nations High Commissioner for Refugees; received the prize twice. Nobel Peace Prize (1954, 1981). Posthumous Nobel Prizes laureates: Erik Axel Karlfeldt; received Nobel Prize in Literature (1931). Dag Hammarskjöld; received Nobel Peace Prize (1961). Ralph M. Steinman; received Nobel Prize in Physiology or Medicine (2011). Married couples to receive Nobel Prizes:[161] Marie Curie, Pierre Curie (along with Henri Becquerel). Received Nobel Prize in Physics (1903). Irène Joliot-Curie, Frédéric Joliot. Received Nobel Prize in Chemistry (1935). Gerty Cori, Carl Cori. Received Nobel Prize in Medicine (1947). Gunnar Myrdal received Nobel Prize in Economics Sciences (1974), Alva Myrdal received Nobel Peace Prize (1982). May-Britt Moser, Edvard I. Moser. Received Nobel Prize in Medicine (2014) Esther Duflo, Abhijit Banerjee (along with Michael Kremer). Received Nobel Prize in Economics Sciences (2019).[162] Specially distinguished laureates Multiple laureates A black and white portrait of a woman in profile. Marie Curie, one of four people who have received the Nobel Prize twice (Physics and Chemistry) Four people have received two Nobel Prizes. Marie Curie received the Physics Prize in 1903 for her work on radioactivity and the Chemistry Prize in 1911 for the isolation of pure radium,[163] making her the only person to be awarded a Nobel Prize in two different sciences. Linus Pauling was awarded the 1954 Chemistry Prize for his research into the chemical bond and its application to the structure of complex substances. Pauling was also awarded the Peace Prize in 1962 for his activism against nuclear weapons, making him the only laureate of two unshared prizes. John Bardeen received the Physics Prize twice: in 1956 for the invention of the transistor and in 1972 for the theory of superconductivity.[164] Frederick Sanger received the prize twice in Chemistry: in 1958 for determining the structure of the insulin molecule and in 1980 for inventing a method of determining base sequences in DNA.[165][166] Two organizations have received the Peace Prize multiple times. The International Committee of the Red Cross received it three times: in 1917 and 1944 for its work during the world wars; and in 1963 during the year of its centenary.[167][168][169] The United Nations High Commissioner for Refugees has been awarded the Peace Prize twice for assisting refugees: in 1954 and 1981.[170] Family laureates The Curie family has received the most prizes, with four prizes awarded to five individual laureates. Marie Curie received the prizes in Physics (in 1903) and Chemistry (in 1911). Her husband, Pierre Curie, shared the 1903 Physics prize with her.[171] Their daughter, Irène Joliot-Curie, received the Chemistry Prize in 1935 together with her husband Frédéric Joliot-Curie. In addition, the husband of Marie Curie's second daughter, Henry Labouisse, was the director of UNICEF when he accepted the Nobel Peace Prize in 1965 on that organisation's behalf.[172] Although no family matches the Curie family's record, there have been several with two laureates. The Nobel Prize in Physiology or Medicine was won by the husband-and-wife team of Gerty Cori and Carl Ferdinand Cori in 1947 Prize,[173] and by the husband-and-wife team of May-Britt Moser and Edvard Moser in 2014 (along with John O'Keefe).[174] The Physics Prize in 1906 was won by J. J. Thomson for showing that electrons are particles, and in 1937 by his son, George Paget Thomson, for showing that they also have the properties of waves.[175] William Henry Bragg and his son, William Lawrence Bragg, shared the Physics Prize in 1915 for inventing the X-ray crystallography.[176] Niels Bohr was awarded the Physics Prize in 1922, as was his son, Aage Bohr, in 1975.[172][177] The Physics Prize was awarded to Manne Siegbahn in 1924, followed by his son, Kai Siegbahn, in 1981.[172][178] Hans von Euler-Chelpin, who received the Chemistry Prize in 1929, was the father of Ulf von Euler, who was awarded the Physiology or Medicine Prize in 1970.[172] C. V. Raman was awarded the Physics Prize in 1930 and was the uncle of Subrahmanyan Chandrasekhar, who was awarded the same prize in 1983.[179][180] Arthur Kornberg received the Physiology or Medicine Prize in 1959; Kornberg's son, Roger later received the Chemistry Prize in 2006.[181] Jan Tinbergen, who was awarded the first Economics Prize in 1969, was the brother of Nikolaas Tinbergen, who received the 1973 Physiology or Medicine Prize.[172] Gunnar Myrdal who was awarded the Economics Prize in 1974, was the husband of Alva Myrdal, Peace Prize laureate in 1982.[172] Economics laureates Paul Samuelson and Kenneth Arrow were brothers-in-law. Frits Zernike, who was awarded the 1953 Physics Prize, is the great-uncle of 1999 Physics laureate Gerard 't Hooft.[182] In 2019, married couple Abhijit Banerjee and Esther Duflo were awarded the Economics Prize.[183] Refusals and constraints A black and white portrait of a man in a suit and tie. Half of his face is in a shadow. Richard Kuhn, who was forced to decline his Nobel Prize in Chemistry Two laureates have voluntarily declined the Nobel Prize. In 1964, Jean-Paul Sartre was awarded the Literature Prize but refused, stating, "A writer must refuse to allow himself to be transformed into an institution, even if it takes place in the most honourable form."[184] Lê Đức Thọ, chosen for the 1973 Peace Prize for his role in the Paris Peace Accords, declined, stating that there was no actual peace in Vietnam.[185] George Bernard Shaw attempted to decline the prize money while accepting the 1925 Literature Prize; eventually it was agreed to use it to found the Anglo-Swedish Literary Foundation.[186] During the Third Reich, Adolf Hitler hindered Richard Kuhn, Adolf Butenandt, and Gerhard Domagk from accepting their prizes. All of them were awarded their diplomas and gold medals after World War II. In 1958, Boris Pasternak declined his prize for literature due to fear of what the Soviet Union government might do if he travelled to Stockholm to accept his prize. In return, the Swedish Academy refused his refusal, saying "this refusal, of course, in no way alters the validity of the award."[185] The academy announced with regret that the presentation of the Literature Prize could not take place that year, holding it back until 1989 when Pasternak's son accepted the prize on his behalf.[187][188] Aung San Suu Kyi was awarded the Nobel Peace Prize in 1991, but her children accepted the prize because she had been placed under house arrest in Burma; Suu Kyi delivered her speech two decades later, in 2012.[189] Liu Xiaobo was awarded the Nobel Peace Prize in 2010 while he and his wife were under house arrest in China as political prisoners, and he was unable to accept the prize in his lifetime. Cultural impact The International Nobel Economic Congress 2008, at the Alfred Nobel University in Dnipro, Ukraine Being a symbol of scientific or literary achievement that is recognisable worldwide, the Nobel Prize is often depicted in fiction. This includes films like The Prize (1963), Nobel Son (2007), and The Wife (2017) about fictional Nobel laureates, as well as fictionalised accounts of stories surrounding real prizes such as Nobel Chor, a 2012 film based on the theft of Rabindranath Tagore's prize.[190][191] The statue and memorial symbol Planet of Alfred Nobel was opened in Alfred Nobel University of Economics and Law in Dnipro, Ukraine in 2008. On the globe, there are 802 Nobel laureates' reliefs made of a composite alloy obtained when disposing of military strategic missiles.[192] Despite the symbolism of intellectual achievement, some recipients have embraced unsupported and pseudoscientific concepts, including various health benefits of vitamin C and other dietary supplements, homeopathy, HIV/AIDS denialism, and various claims about race and intelligence.[193] This is sometimes referred to as Nobel disease. See also image History of Science portal flag Norway portal flag Sweden portal List of Nobel laureates List of female Nobel laureates List of Nobel laureates by country List of Nobel laureates by secondary school affiliation List of Nobel laureates in Chemistry List of Nobel laureates in Literature List of Nobel Peace Prize laureates List of Nobel laureates in Physics List of Nobel laureates in Physiology or Medicine List of Nobel Memorial Prize laureates in Economics Fields Medal – Mathematics award Ig Nobel Prize – Annually awarded parody of the Nobel Prize Lindau Nobel Laureate Meetings List of prizes known as the Nobel of a field Lists of science and technology awards Nobel Conference Nobel Library Nobel Prize Museum – Museum about Alfred Nobel and the Nobel Prize Nobel Prize effect – Observation about the adverse effects of receiving the Nobel Prize References
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