John Kendrew

For more information on Sir John Cowdery Kendrew, visit Britannica.com.

British biochemist (1917–1997)

Kendrew, who was born at Oxford, graduated in natural science from Cambridge University in 1939. He spent the war years working for the Ministry of Aircraft Production, becoming an honorary wing commander in 1944. In 1946 he joined Max Perutz at Cambridge and, like Perutz, used x-ray diffraction techniques to study the crystalline structure of proteins, particularly that of the muscle protein myoglobin. X-ray diffraction, or crystallography, involves placing a crystal in front of a photographic plate and rotating the crystal in a beam of x-rays. The pattern of dots that is formed on the plate by the x-rays can be analyzed to find the positions of the atoms in the crystal. The technique had been used successfully to show the structures of small molecules but Kendrew's progress with the much larger myoglobin structure was slow, especially since diffraction patterns yield no information on the phases of the directed x-rays. However, in 1953 Perutz made a breakthrough by incorporating atoms of heavy elements into the protein crystals. Kendrew modified this new method and applied it successfully in his myoglobin studies, so that four years later he had built up a rough model of the three-dimensional structure of myoglobin. By 1959 he had greatly clarified the structure and could pinpoint most of the atoms.

Kendrew and Perutz received the 1962 Nobel Prize for chemistry for their work on protein structure. Kendrew was knighted in 1974 and served as director general of the European Molecular Biology Laboratory in Heidelberg from 1975 to 1982.

John C. Kendrew (born 1917) was awarded the Nobel Prize in chemistry (with Max Perutz) in 1962 for his work in determining protein structures.

John Cowdery Kendrew was born in Oxford, England, on March 24, 1917, the son of Wilfred George and Evelyn May Graham (Sandberg) Kendrew. His father was a climatologist at the university; thus young Kendrew was raised in a highly enriched, scientific atmosphere. He trained as a physical chemist upon entering Cambridge, taking his B.A. from Trinity College in the spring of 1939. After graduation he considered switching to biology for further study, but without clear direction, and with the outbreak of World War II he joined the Air Ministry and worked on the application of airborne radar to the war effort and as a civilian scientist for the Royal Air Force. Kendrew worked for the RAF until 1945, first in England, then in the Middle East, and finally in Southeast Asia.

Early Interest in Structural Chemistry

It was in the Far East that he first became acquainted with J. D. Bernal, the great structural chemist and later scientific adviser to Lord Mountbatten. Ironically, Bernal had been working at Cambridge throughout the 1930s utilizing x-ray diffraction to determine the structure of crystals. This is accomplished by directing a beam of x-rays upon a crystal and capturing the diffraction pattern established upon a photographic plate. Bernal was at that time excited about the possibility of determining the structure of proteins through the use of x-rays, and he convinced Kendrew that the field was ready for cultivation. Kendrew's mind was thus at work upon structures when, on a military trip to California, he met Linus Pauling and learned of his interest in protein and amino acid structures. The combined influence of Bernal and Pauling persuaded him to switch from chemistry to biology, and with the war's end he returned to Cambridge to pursue his doctorate.

Work with Myoglobin

Max Perutz, a former student of Bernal's, was already working on the structure of hemoglobin at Cambridge's Cavendish Laboratory when Kendrew joined him in 1946. From Perutz he learned the elements of crystallography, and he began his doctoral research on the protein myoglobin. Kendrew chose this protein because of its close relation to hemoglobin, but also because it was one-quarter the size (2,500 atoms to hemoglobin's 10,000). While actively engaged in this research, and though he had not yet finished his doctoral requirements, Kendrew rose rapidly in the post-war academic hierarchy. In 1947 he was named department chairman of the Medical Research Council Laboratory for Molecular Biology, also in the Cavendish Laboratory under Sir Lawrence Bragg but later in its own building, a post he held at Cambridge until 1975 - a period concurrent with his being a fellow of Peterhouse. In 1949 he finished his Ph.D., but he continued to work on the structure of myoglobin as the determination of its crystalline arrangement was still unsolved.

In 1953 Perutz discovered a new technique that was to unravel the mystery of the protein. He showed that attaching a single atom, such as gold or mercury, to a hemoglobin molecule slightly altered the diffraction pattern. By a comparison of before and after photographs it was possible to determine the heavy atoms' positions in the hemoglobin crystal. This method, known as isomorphic replacement, could potentially solve the entire puzzle of hemoglobin structure. Kendrew applied it to the simpler molecule myoglobin, succeeding by 1957 - after thousands of photographs and repeated measurements - in unraveling the first protein structure. This first picture was rather blurred, but by 1959, after many more photographs and measurements, Kendrew and his associates achieved a very high resolution, such that most of the individual atoms were now "visible." Eventually, nearly every atom's location in the molecule was determined, but at the time the polypeptide chain was shown to coil about in a spiral manner already described theoretically by Pauling in 1951 and called the alpha-helix.

For their work Perutz and Kendrew were awarded the 1962 Nobel Prize in chemistry. Kendrew received other recognition for his work in what is now commonly known as molecular biology - a 1960 fellow of the Royal Society; decorated knight bachelor and commander, Order of the British Empire; and foreign associate, National Academy of Sciences (United States). After 1959 he was editor-in-chief of the Journal for Molecular Biology, and in 1970 he left Cambridge for the post of director-general of the European Molecular Biology Laboratory in Heidelberg, Germany, which he held until 1982.

Further Reading

Horace Judson's The Eighth Day of Creation (1979) tells the story of molecular biology; the Thread of Life (1966), by Kendrew, non-technical overview with x-ray crystallographic photographs. See also: "How Molecular Biology Got Started" in Scientific American, vol. 216, 1967, pp. 141-143; and "Myoglobin and the Structure of Proteins (Nobel Address)" in Science, Vol. 139, 1963, pp. 1259 -1266; Biochemistry by Lubert Stryer (1988).

For the Industrial Revolution-era designer, see John Kendrew (inventor).

John Cowdery Kendrew
Born	24 March 1917 Oxford, England
Died	23 August 1997 (aged 80) Cambridge, England
Nationality	United Kingdom
Fields	Crystallography
Institutions	Royal Air Force
Alma mater	University of Cambridge
Doctoral advisor	Max Perutz
Known for	Heme-containing proteins
Notable awards	Nobel Prize for Chemistry (1962)

This article includes a list of references, related reading or external links, but its sources remain unclear because it lacks inline citations. Please improve this article by introducing more precise citations where appropriate. (September 2009)

Sir John Cowdery Kendrew, CBE, FRS (24 March 1917 – 23 August 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.

Contents 1 Biography 1.1 Crystallography 1.2 Crystal structure of myoglobin 1.3 Later career 2 References 3 Publications 4 External links

Biography

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 the Medical Research Council(MRC) 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

John Kendrew with model of myoglobin in progress. Copyright by the Laboratory of Molecular Biology in Cambridge, England.

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 stores oxygen in muscle cells. On Saturday 20 October 1962 the award of Nobel prizes to John Kendrew and Max Perutz, and to Crick, Watson, and Wilkins was satirised in a short sketch in the BBC TV programme That Was The Week That Was with the Nobel Prizes being referred to as 'The Alfred Nobel Peace Pools'.

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. Whale myoglobin did give large crystals with clean X-ray diffraction patterns. However, the problem still remained insurmountable, until in 1953 Max Perutz discovered that the phase problem in analysis of the diffraction patterns could be solved by multiple isomorphous replacement — comparison of patterns from several crystals; one from the native protein, and others that had been soaked in solutions of heavy metals and had metal ions introduced in different well-defined positions. An electron density map at 6 angstrom (0.6 nanometre) resolution was obtained by 1957, and by 1959 an atomic model could be built at 2 angstrom (0.2 nm) 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 and honorary member of the International Academy of Science. In 1974 he succeeded in persuading governments to establish the European Molecular Biology Laboratory 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.

After his retirement from the European Molecular Biology Laboratory, Kendrew became President of St. John's College, Oxford, a post he held from 1981-1987. From 1974-79 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. Kendrew's entry in Who's Who lists ten other important National and International committees on which he served as either member or chairman.

References

• John Finch; 'A Nobel Fellow On Every Floor', Medical Research Council 2008, 381 pp, ISBN 978-1840469-40-0; this book is all about the MRC Laboratory of Molecular Biology, Cambridge.

Publications

• Kendrew, JC (Oct 1962). "The structure of globular proteins". Comparative biochemistry and physiology 4: 249–52. doi:10.1016/0010-406X(62)90009-9. ISSN 0010-406X. PMID 14031911. 
• Kendrew, JC (Dec 1961). "The three-dimensional structure of a protein molecule". Scientific American 205: 96–110. ISSN 0036-8733. PMID 14455128. 
• Watson, HC; Kendrew (May 1961). "The amino-acid sequence of sperm whale myoglobin. Comparison between the amino-acid sequences of sperm whale myoglobin and of human hemoglobin". Nature 190: 670–2. doi:10.1038/190670a0. ISSN 0028-0836. PMID 13783432. 
• Kendrew, JC; Watson; Strandberg; Dickerson; Phillips; Shore (May 1961). "The amino-acid sequence x-ray methods, and its correlation with chemical data". Nature 190: 666–70. doi:10.1038/190666a0. ISSN 0028-0836. PMID 13752474. 
• Kendrew, JC (Jul 1959). "Structure and function in myoglobin and other proteins". Federation proceedings 18 (2, Part 1): 740–51. ISSN 0014-9446. PMID 13672267. 
• Kendrew, JC; Bodo; Dintzis; Parrish; Wyckoff; Phillips (Mar 1958). "A three-dimensional model of the myoglobin molecule obtained by x-ray analysis". Nature 181 (4610): 662–6. doi:10.1038/181662a0. ISSN 0028-0836. PMID 13517261. 
• Ingram, DJ; Kendrew (Oct 1956). "Orientation of the haem group in myoglobin and its relation to the polypeptide chain direction". Nature 178 (4539): 905–6. doi:10.1038/178905a0. ISSN 0028-0836. PMID 13369569. 
• Kendrew, JC; Parris (Jan 1955). "Imidazole complexes of myoglobin and the position of the haem group". Nature 175 (4448): 206–7. doi:10.1038/175206b0. ISSN 0028-0836. PMID 13235845. 
• Kendrew, JC; Parrish; Marrack; Orlans (Nov 1954). "The species specificity of myoglobin". Nature 174 (4438): 946–9. doi:10.1038/174946a0. ISSN 0028-0836. PMID 13214049. 
• Kendrew, JC (Apr 1949). "Foetal haemoglobin". Endeavour 8 (30): 80–5. ISSN 0160-9327. PMID 18144277. 
• Kendrew, John C. (1966). The thread of life: an introduction to molecular biology. London: Bell & Hyman. ISBN 978-0-7135-0618-1. 

External links

• Max Perutz obituary of John Kendrew
• Nobel website biography

v • d • e Nobel Laureates in Chemistry Edwin McMillan / Glenn T. Seaborg (1951) · Archer Martin / Richard Synge (1952) · Hermann Staudinger (1953) · Linus Pauling (1954) · Vincent du Vigneaud (1955) · Cyril Hinshelwood / Nikolay Semyonov (1956) · Alexander Todd (1957) · Frederick Sanger (1958) · Jaroslav Heyrovský (1959) · Willard Libby (1960) · Melvin Calvin (1961) · Max Perutz / John Kendrew (1962) · Karl Ziegler / Giulio Natta (1963) · Dorothy Hodgkin (1964) · Robert Woodward (1965) · Robert S. Mulliken (1966) · Manfred Eigen / Ronald Norrish / George Porter (1967) · Lars Onsager (1968) · Derek Barton / Odd Hassel (1969) · Luis Federico Leloir (1970) · Gerhard Herzberg (1971) · Christian B. Anfinsen / Stanford Moore / William Stein (1972) · E.O.Fischer / Geoffrey Wilkinson (1973) · Paul Flory (1974) · John Cornforth / Vladimir Prelog (1975) Complete roster · 1901–1925 · 1926–1950 · 1951–1975 · 1976–2000 · 2001–present

Persondata
NAME	Kendrew, John Cowdery
ALTERNATIVE NAMES
SHORT DESCRIPTION	English biochemist and crystallographer who shared the 1962 Nobel Prize in Chemistry with Max Perutz
DATE OF BIRTH	24 March 1917
PLACE OF BIRTH	Oxford, England
DATE OF DEATH	1997-8-23
PLACE OF DEATH	Cambridge, England

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