John Kendrew

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John Kendrew

John Cowdery Kendrew (March 24, 1917 – August 23, 1997) was an English biochemist, crystallographer, and Nobel prize winner in the field of chemistry in 1962, a prize shared with Max Perutz, whose group in the Cavendish Laboratory was involved in the investigation of 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. Dr. Joseph Barcroft, 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 diffraction pattern

Kendrew 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 ths study progressed as far as possible in the context of the time, Kendrew embarked on the study of myoglobin, only 1/4 of the size of the hemoglobin molecule. Horse heart was the initial source of material, but crystals were too small for X-ray analysis. Kendrew realized that diving mammals offered a better prospect, and a chance encounter enabled the procurement of a large chunk of whale meat from Peru, and this gave large crystals with beautiful 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

References

• [Nobel website biography]

External links

• Max Perutz [obituary] of John Kendrew

Bibliography

• Thread of Life by Sir John Kendrew: (ISBN 0713506180) G.Bell, 1966;

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