`John Cowdery Kendrew` Biography - Nobel Prize Winner (1962)

John Cowdery Kendrew (March 24, 1917 – August 23, 1997) was an English biochemist and crystallographer who shared the 1962 Nobel Prize in Chemistry with Max Perutz; their group in the Cavendish Laboratory investigated the structure of heme-containing proteins. Early life He was born in Oxford, son of Wilford George Kendrew, reader in climatology in the University of Oxford and Evelyn May Graham Sandburg, art historian. He was educated at the Dragon School in Oxford, as well as Clifton College in Bristol, 1930-1936. He attended Trinity College, Cambridge in 1936, as a Major Scholar, graduating in chemistry in 1939. He spent the early months of World War II doing research on reaction kinetics, and then became a member of the Air Ministry Research Establishment, working on radar. In 1940 he became engaged in operational research at the Royal Air Force headquarters, holding the honorary rank of Wing Commander R.A.F. During the war years, he became increasingly interested in biochemical problems, and decided to work on the structure of proteins. Crystallography In 1945 he approached Dr. Max Perutz in the Cavendish Laboratory in Cambridge. Joseph Barcroft, a respiratory physiologist, suggested he might make a comparative protein crystallographic study of adult and fetal sheep hemoglobin, and he started that work. In 1947 he became a Fellow of Peterhouse, and MRC [the Medical Research Council] agreed to create a research unit for the study of the molecular structure of biological systems, under the direction of Sir Lawrence Bragg. In 1954 he became a Reader at the Davy-Faraday Laboratory of the Royal Institution in London. Crystal structure of myoglobin Myoglobin diffraction patternKendrew shared the 1962 Nobel Prize for chemistry with Max Perutz for determining the first atomic structures of proteins using X-ray crystallography. Their work was done at what is now the MRC Laboratory of Molecular Biology in Cambridge. Kendrew determined the structure of the protein myoglobin, which transports oxygen in muscle cells. In 1947 the MRC agreed to make a research unit for the Study of the Molecular Structure of Biological Systems. The original studies were on the structure of sheep hemoglobin, but when this work had progressed as far as was possible using the resources then available, Kendrew embarked on the study of myoglobin, a molecule only a quarter the size of the hemoglobin molecule. His initial source of raw material was horse heart, but the crystals thus obtained were too small for X-ray analysis. Kendrew realized that the oxygen-conserving tissue of diving mammals could offer a better prospect, and a chance encounter led to his acquiring a large chunk of whale meat from Peru. The whale-sourced myoglobin gave large crystals with clean X-ray diffraction patterns. However, the problem still remained insoluble, until in 1953 Max Perutz discovered that the phase problem in analysis of the diffraction patterns could be solved by comparison of patterns from two crystals - one from the native protein, and one from the protein with heavy metals attached to it. An electron density at 6 Angstroms resolution was obtained by 1957, and by 1959 an atomic model could be built at 2 Angstroms resolution. Later career In 1963 Kendrew became one of the founders of the European Molecular Biology Organization; as well, he founded and was for many years editor-in-chief of the Journal of Molecular Biology. He became Fellow of the American Society of Biological Chemists in 1967. In 1974 he succeeded in persuading governments to build a European Laboratory of Molecular Biology in Heidelberg and became its first director. From 1974 to 1979 he was a Trustee of the British Museum, and from 1974 to 1988 he was successively Secretary General, Vice-President, and President of the International Council of Scientific Unions.

LIST OF NOBEL PRIZE WINNERS IN CHEMISTRY PART II.

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