Kendra (Kendrew), John K.( English biochemist, Nobel Prize in Chemistry, 1962)
Comments for Kendra (Kendrew), John K.
Biography Kendra (Kendrew), John K.
genus. March 24, 1917
English biochemist John Cowdery Kendrew was born in Oxford. He was the only son of Wilfrid George Kendrew, . known climatologist, . who taught at Oxford University, . and Evelyn Mae Graham (Sandburg) Kendrew, . art historian, . by Italian artists-primitivist and published several papers on this topic,
. The boy first went to Dragon School in Oxford, and then to Clifton College in Bristol. By the time the Clifton College, he decided to make a career scientist and went to Cambridge University, despite the fact that his father was associated with Oxford. In 1939, Mr.. K. earned a bachelor of science, and in 1943. - Master.
A year after in 1939. Britain announced that it is in a state of war with Germany, to. joined the Ministry of Aviation Industry as a junior officer and researcher. In 1944, Mr.. he became scientific advisor to the commander in chief of the Air Force allies, based in South-East Asia. Toward the end of the Second World War, after meeting with British chemist Dzh.D. Bernal and the American chemist Linus K. Polito, K. interested in the molecular structure of proteins. After leaving government service, he returned in 1946. in Cambridge and began working with Max Perutz at the Cavendish Laboratory. In 1949, Mr.. K. received his doctorate in philosophy, and in 1962. He received his Doctor of Natural Sciences.
At a time when K. began working at the Cavendish Laboratory, Perutz returned to his earlier studies of the molecular structure of proteins of red blood cells using the method of X-ray crystallography. This method consists in the fact that the X-ray beam passes through the crystal and recorded on a photographic plate. Since the rays are deflected by electrons of the atoms of the crystal, the picture that is formed on the plate, allows to reveal its atomic structure.
While Perutz continued to study hemoglobin, K. attempted to establish the structure of myoglobin - a substance that stores oxygen in the muscles of animals and humans. Despite the fact that the structure of myoglobin is much simpler than the structure of hemoglobin, in his study nevertheless far from easy, because it consists of approximately 50 amino acids, ie. approximately 2600 atoms. The task of determining the location of these atoms is further complicated by the fact that the method of X-ray crystallography has depended to a large extent on the correct interpretation of the data.
In 1947, Mr.. K. followed Perutz went to work in a group of Molecular Biology, created in the same year at the Cavendish Laboratory of the Medical Research Council. First K. and Perutz worked just in the barn together. Later they were joined by Francis Crick, James D. Watson, Frederick Sanger, and other scientists.
Work to. of myoglobin was decisive impetus when in 1953. Perutz discovered that the introduction of mercury atoms in the crystals of hemoglobin changes the diffraction pattern obtained by X-ray emission. Comparing the first retrieve and modify the picture, it was possible to establish the structure of the molecule. Applying the method of isomorphous replacement (introducing atoms of heavy metals in the molecule of crystalline proteins) to their own research to. found that myoglobin 'does not deter' mercury atoms, and was forced to seek to replace the atoms of other heavy metals.
. The diffraction pattern spots located on the plate closest to the center, by radioactive rays reflected far-spaced atoms, and it is at these spots to the
. and his colleagues focused their attention. By 1957, Mr.. they can distinguish objects located at a distance of six angstrom (6.10 -10 m). Despite the fact that at such a scale the diffraction pattern does not reveal individual atoms, they still saw 'something that nobody had not previously noticed - later recalled to. - It was a three-dimensional structure of protein molecules in all its complexity '.
The work of Frederick Sanger had recently shown that proteins are composed of arranged in a chain of amino acids linked chemical bond called the peptide. Subject to distinguish objects at a distance of 6 angstrom to. able to establish a spiral pattern of the polypeptide chain of myoglobin. 'The most striking feature of this molecule, - he reported - was its orderliness and the complete lack of symmetry'. These features are further clarified in 1959, when K. received image myoglobin molecule, provided the resolution of a 2 angstrom - an achievement made possible through the use of powerful computers needed to carry out mathematical calculations.
In 1962. K. and Perutz was awarded the Nobel Prize in Chemistry 'for studying the structure of globular proteins'. 'Proteins are unique in the sense that they combine the tremendous variety of functions and complexity of construction with relative simplicity and uniformity of the chemical structure', - said to. in his Nobel lecture. 'The establishment of the structures of only two proteins, we have achieved - is not the end but the beginning - he went. - Before we came ashore vast continent waiting for their researchers'.
From 1953 to 1974. K. was deputy director of the Laboratory of Molecular Biology (formerly the Group of Molecular Biology) in Cambridge, and in 1975. became the first director of the European Molecular Biology Laboratory in Heidelberg (Germany). This post he held until 1982. In 1981. scientist was elected president of the College of St.. John Oxford University. K. single. He is spoken of as an impressionable man, quiet and modest. In his spare time he likes to listen to music, brought together an important collection of recordings of classical music.
In addition to the Nobel Prize, K. awarded the Royal Medal of Royal Society of London (1965). In 1963, Mr.. He was ordained to the peers. Scientist - a member of the British Association for the Advancement of Science, and from 1974 to 1979. - Trustee of the British Museum. He is an honorary member of the American Academy of Arts and Sciences, Germanskoy Academy of Natural Scientists 'Leopoldina', the Heidelberg Academy of Sciences, Bulgarian Academy of Sciences and the Royal Irish Academy of Sciences. K. holds honorary degrees from universities of Kiel, Reading, Bekingema and Exeter.