John Cowdery Kendrew | Biography

The decades following World War II saw an increase in using physical methods to solve biological problems, which led to a greatly increased knowledge of living systems. John Kendrew's contribution to this trend was formulating the first three-dimensional structure of the protein myoglobin by using x-ray crystallography. For this achievement he shared the 1962 Nobel Prize in chemistry with his colleague Max Perutz, who had done similar work with hemoglobin.

Kendrew was born in Oxford, England, the only child of Wilfrid and Evelyn Sandberg Kendrew. His father was a lecturer in climatology, and his mother was an art historian; thus he was nurtured in an academic atmosphere. He attended the Dragon School in Oxford and finished his secondary schooling at Clifton College in Bristol. He matriculated at Trinity College, Cambridge, where he studied chemistry and graduated in 1939.

Kendrew's academic career was interrupted by World War II, when he served with the Ministry of Aircraft Production. He worked for a time on radar, and then acted as scientific advisor to the Allied air commander in chief in Southeast Asia. While serving in Asia, Kendrew met physicist J. D. Bernal. Bernal was convinced that the intersection between biology and the physical sciences would soon be an important area of research, and this greatly influenced Kendrew's career path. On a side trip to California, Kendrew also met the American physical chemist Linus Pauling, whose protein work would later serve as a foundation for his own.

After the war Kendrew became a doctoral candidate at the Cavendish Laboratory at Cambridge where he met Perutz, who had once been a student of Bernal's. Together they worked under physicist Lawrence Bragg, who had helped establish the science of x-ray crystallography (a process that outlines a substance's atomic structure) in the early twentieth century. By 1947, Bragg had convinced the secretary of the medical research council that the government should finance the kind of work that Kendrew and Perutz were doing. A special unit for the study of the molecular structure of biological systems was founded for the two scientists, housed in an empty shed at Cambridge.

Kendrew's doctoral thesis dealt with the differences between fetal and adult sheep hemoglobin, a component of red blood cells that contains iron and assists with oxygen transport. The project gave him valuable experience in x-ray methods and a chance to work with proteins, which he came to regard as the most important class of biological molecules. After receiving his Ph.D. in 1949, Kendrew commenced research on the protein myoglobin. Myoglobin is the molecule that binds and transports oxygen in the muscles, and was readily available from whales. Perutz was already working on determining the structure of hemoglobin. At the time Kendrew started his research, little was known about myoglobin, except that it was a protein.

The first problem Kendrew faced was to produce crystals of pure myoglobin. To do this, he planned to use x-ray crystallography, which required samples with regular crystal structures. The technique involved shining x rays through the crystal and observing on photographic paper the pattern of spots that leaves the crystal. The atoms in the crystal diffract the x rays through definite angles, concentrating them in patterns of bands or spots from which the scientist must calculate the kind of atomic arrangement that produced such a pattern.

Kendrew and his colleagues obtained their crystals, and x-ray pictures of them, but the pictures proved to be too complex to interpret. Fortunately, Perutz recalled a technique he had learned from Bernal in which a heavy metal atom bonded with a protein to serve as a marker so that the diffracted x rays could be sorted out. Kendrew, however, had to try a number of heavy metals before he could make interpretable pictures; in all he made well over ten-thousand images. When he finally had the laboratory data he wanted, he made his mathematical calculations of electron densities with a computer.

Even after Kendrew obtained his densities, a formidable problem remained. The densities had to be plotted for planar slices through the crystal at intervals of a few angstrom units (one ten-billionth of a meter), and the contours of electron density (like elevations on a topographical map) had to be determined. High density indicated an atom, and certain atoms (like nitrogen and oxygen) could be distinguished by the magnitude of their density. Since computers were not yet capable of these calculations, Kendrick's group had to do all the plotting by hand. They announced their findings in 1960, in the same issue of Nature in which Perutz published his preliminary findings on hemoglobin.

The myoglobin molecule proved to be a dense, lumpy structure. It had none of the beauty and regularity that molecular biologists Francis Crick and James Watson had found in their x-ray work on deoxyribonucleic acid (DNA), for which they received the Nobel Prize in medicine or physiology in 1962--the same year that Kendrew and Perutz were awarded the Nobel Prize in chemistry. One writer commented that the significance of Kendrew's work lay not in the new insights it provided, but in the fact that it could be done at all. Kendrew had risked analyzing a complex structure when many simpler ones had not yet been attempted, and he had succeeded.

Although Kendrew continued his work on the structure of myoglobin after receiving the Nobel Prize, he was increasingly drawn into administration and government advisory positions. The department Kendrew and Perutz created at Cambridge was now known as the Laboratory for Molecular Biology, and Kendrew acted as deputy chairman of the organization from its inception until 1974. The following year he established the European Molecular Biology Laboratory in Heidelberg, Germany, and served as its director until 1982. Earlier in his career he founded the Journal of Molecular Biology and acted as its editor-in-chief until 1987. From 1954 to 1968 he was a reader at the Davy-Faraday Laboratory of the Royal Institution, London, and from 1981 to 1987 he was president of St. John's College, Oxford. In addition, he has served as president of the International Organization of Pure and Applied Biophysics, and as both secretary general and president of the International Council of Scientific Unions.

Kendrew has been recognized for his achievements with many awards in addition to his Nobel Prize. He is an honorary fellow of Peterhouse, Cambridge, and St. John's, Oxford. He is also a fellow of the Royal Society, a foreign associate of the National Academy of Sciences in the United States, and a foreign honorary member of the American Academy of Arts and Sciences. He was knighted and given the Order of the British Empire in 1963.