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Perutz (Perutz), Max

( English biochemist, Nobel Prize in Chemistry, 1962)

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Biography Perutz (Perutz), Max
genus. May 19, 1914
English biochemist Max Ferdinand Perutz was born in Austria, Vienna. He was one of three children, Adele (Goldsmith) and Hugo Perutz Perutz. Parents PP, which came from a wealthy family of textile manufacturers, hoping that Max will study law and engage in family business. However, when P. attended high school in Vienna, he developed an interest in chemistry. In 1932, Mr.. he entered the University of Vienna in the department of inorganic chemistry, but soon discovered that this subject is not interested in him, and moved to separate organic chemistry. It is engaged in organic matter, P. first learned about research in the field of X-ray crystallography, which then held at Cambridge University. After graduating from a university course in Vienna in 1936, he moved to Cambridge to work with the famous physicist Dzh.D. Bernal at the Cavendish Laboratory.
Method of X-ray crystallography began in 1912, when Max von Laue, X-ray beam passing through the crystal on the photographic plate, was now dark spots. This diffraction pattern - the name under which it is now known - have different for different kinds of crystals. Two years later U.G. Bragg and U.L. Bragg found that, because X-rays are deflected by atoms of the crystal, with the help of mathematical methods can process the results of the diffraction pattern and to establish the atomic structure of the test material.
. Father and son Bragg studied quite simple crystals, such as sodium chloride (salt), which consist of only a few kinds of atoms
. Bernal also interested in much more complex structure of proteins, and he hoped that the study using the diffraction pattern in the end will allow him to understand the function of specific protein. In 1937, having studied the method of X-ray diffraction from Bernal and physicist Isidor Fankyuhena, P. initiated a study of hemoglobin - carries oxygen globular protein of blood.
In 1938, shortly after the P. began work on hemoglobin, Bernal left the University of London. A year later, because of the annexation of Austria by the Nazis P. lost the financial support from parents. U.L. Bragg, who had recently started working at Cambridge University, helped him obtain a grant from the Rockefeller Foundation. Thanks to P. remained at the university as an assistant researcher Bragg and in 1940. received his doctorate. The following year, P. was interned in Canada as a citizen of a hostile state. Nevertheless, his interest in the crystalline properties of glaciers led to the fact that in 1943. He was appointed member of a secret project allies, in which he led by Lord Louis Mountbatten's explore the possibilities of the ice fields as airfields. This project, however, was never implemented.
After the war, P. received research fellowships from the 'Imperial Chemical Industries' and returned to the study of hemoglobin in the Cavendish Laboratory. Two years later, when the term of the stipend was over, he was appointed head of molecular biology at Cambridge University, established in 1947. Medical Research Council. Initially, his only colleague was John K. Kendrew, who was then preparing a doctoral thesis and investigated by X-ray myoglobin - substances that stores oxygen in the muscles of animals and humans. When the state of molecular biology with the arrival of Francis Crick in 1949. and James D. Watson in 1951. increased P. and his colleagues have been looking for ordering in the structure of protein molecules. If they were able to establish that such an ordering does exist, it would be possible to decipher the structure of the crystalline protein by constructing his model by trial and error.
This problem P. decided only in 1953, using as the main method of X-ray crystallography, known as method of isomorphous replacement. With this method, the atom of heavy metal such as mercury, is introduced into the molecule of crystalline protein adherence to a particular atom. The atoms of the heavy metal causes a greater deviation of X-rays, and, consequently, a different diffraction pattern is obtained. Comparing these two pictures, you can set the location of specific atoms and thus to extract important information about the structure of the crystal.
By 1956,. P. received a half-dozen types of hemoglobin molecules, each with a heavy metal atom is located in different places. Over the next four years the scientist has collected thousands of photographic plates and processed them the results obtained with the help of computers, and in 1960. proposed a model three-dimensional structure of hemoglobin. The results of his research were published in February of that year in the British journal 'Nature' ( 'Nature'), together with the discoveries Kendrew, which related to myoglobin molecule.
In 1962. P. and Kendrew were awarded the Nobel Prize in Chemistry 'for studying the structure of globular proteins'. 'As a result, the contribution of P. and Kendrew, - said Gunnar Haggai in his opening speech on behalf of the Royal Swedish Academy of Sciences - an opportunity to see the principles underlying the structure of globular proteins'. This achievement, he continued, 'means a big step forward in the understanding of life processes'. In his Nobel lecture P. stressed, . that the 'discovery of a significant structural change, . which is accompanied by the reaction of hemoglobin with oxygen, . suggests, . that there may be other enzymes, . change its structure in becoming a substrate, . and this, . perhaps, . is an important factor in determining the enzymatic catalysis'.,
. After receiving the Nobel Prize P
. continued his study of globular proteins. By optimizing the model they created a molecule of hemoglobin, he was able to show how this structure operates by transferring oxygen in the blood. Despite the fact that P. resigned from his post as head of the Laboratory of Molecular Biology (formerly the group of Molecular Biology) in 1979, he remains actively involved in the study of hemoglobin.
In 1942, Mr.. P. married Gisela Clara Peizerat, who worked as a photographer of Medical Service. In the couple have a son and daughter. At one time, an avid skier and mountaineer, P. described his interest in the glaciers 'mainly as an excuse to work in the mountains'. AP, which speak as someone shy and timid, among his colleagues has proved extremely tenacious researcher.
P. served as a consultant to the British Ministry of Defense, from 1963 to 1969,. was chairman of the European Molecular Biology Organization, and in 1974 ... 1979. - Professor of physiology at the Royal Institution in London. He was awarded the Royal Medal (1971) and Copley Medal (1979) Royal Society of London. The scientist - a foreign member of the French Academy of Sciences and the American National Academy of Sciences. He was awarded honorary degrees from universities of Edinburgh, Norwich, Salzburg and Vienna.

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