John Kendrew Biography

John Cowdery Kendrew was born on 24 March 1917, in Oxford, Oxfordshire, England. His father Wilfrid George Kendrew was a reader in climatology at the ‘University of Oxford.’ His mother Evelyn May Graham Sandburg was an art historian. For many years, she lived in Florence where she published works on the ‘Italian Primitives.’

In 1923, John Kendrew began his education at ‘Dragon School,’ a well-known preparatory school in Oxford. He studied there until 1930. Afterwards, he was sent to ‘Clifton College,’ a co-educational independent school located in the port city of Bristol, for his secondary education.

At ‘Clifton College,’ special emphasis was laid on science, rather than classical studies, as per the norm those days. He passed out from there in 1936 and subsequently, received admission at ‘Trinity College,’ Cambridge.

In due course, he took up the ‘Tripos Part I’ in Chemistry, Physics, Mathematics, and Biochemistry and became a senior scholar in natural sciences. Finally, he graduated in 1939, taking ‘Tripos Part II’ in Chemistry. Soon after his graduation, ‘World War II’ broke out and Great Britain got involved in the war.

During the first few months of the war, John Kendrew researched on reaction kinetics under the supervision of Dr. E.A. Moelwyn Hughes. Subsequently, he became a member of the ‘Air Ministry Research Establishment,’ which was later renamed ‘Telecommunications Research Establishment.’ Here, he worked mainly on radar.

From 1940, Kendrew began working on operation research under Sir Robert Watson-Watt at the ‘Royal Air Force Headquarters’ where he held the honorary rank of wing commander. Later, he was posted in places like the Middle East and South East Asia.

While in Ceylon (now Sri Lanka), he met John Desmond Bernal, the great structural chemist who later became a scientific adviser to Lord Mountbatten. On his way back to England, after the surrender of Japan, he also met Linus Pauling at the ‘California Institute of Technology,’ Pasadena.

John Desmond Bernal and Linus Pauling were greatly interested in protein and persuaded Kendrew to switch to biology. Influenced by their knowledge and enthusiasm, Kendrew decided to start working on the structure of proteins. He started working on it even before reaching England.

In 1946, after coming back to England, John Cowdery Kendrew approached Max Ferdinand Perutz. Perutz was a student of John Desmond Bernal and was working on the structure of hemoglobin at ‘Cavendish Laboratory’ at the time.

Around this time, he also met Joseph Barcroft, an English physiologist, best known for his study on oxygenation of blood. Barcroft suggested that Kendrew could make a comparative protein crystallographic study of adult and fetal sheep hemoglobin.

In 1947, while he was still working on his doctoral thesis, Kendrew became a Fellow of Peterhouse. In the same year, he and Perutz established ‘Medical Research Council Unit for Molecular Biology’ in ‘Cavendish Laboratory’ under the guidance of Sir Lawrence Bragg. Subsequently, Kendrew became its deputy chairman and held the position till 1975.

Meanwhile, Kendrew and Perutz continued their work on the structure of sheep hemoglobin. Later, when resources became scarce, Kendrew began to work on myoglobin, an iron and oxygen binding protein found in the muscle tissue of vertebrates. It is closely related to hemoglobin, but is much smaller in size.

In 1949, Kendrew received his PhD degree. But he carried on his work on the structure of myoglobin as he was yet to determine its crystalline arrangement. Initially, he faced a lot of problems determining myoglobin’s crystalline arrangement.

In 1953, Perutz discovered a new technique called ‘multiple isomorphous replacement’ (MIR) that was capable of solving the phase problem. Kendrew applied this technique to the simpler molecule myoglobin.

Before Kendrew could succeed in this project, he and Perutz moved with Bragg to the ‘Royal Institution’ in London. In 1954, he and Perutz were appointed honorary readers of ‘Davy Faraday Research Laboratory’ at the ‘Royal Institution.’ They held their respective posts till 1968.

Meanwhile, they continued with their research work. In 1957, after taking thousands of photographs and measurements, Kendrew was able to unravel the structure of protein myoglobin. However, the pictures were not clear and therefore Kendrew kept working on them.

By 1959, Kendrew was able to take high resolution pictures. Most of the atoms in the myoglobin molecule were now clearly visible. He worked further and was soon able to determine the location of each atom in the molecule.

Perutz, who had been working on hemoglobin, was also able to describe its structure. More importantly, he was able to locate the helical chains in hemoglobin; Kendrew had found the helical chains in myoglobin. This stimulated activity in molecular biology all over the world.

Starting from the 1960s, Kendrew became more interested in policy matters than in direct research. In 1963, he started working towards the establishment of ‘European Molecular Biology Organization,’ becoming its founder member in July 1964.

In 1974, he successfully persuaded governments of different European countries to establish a ‘European Molecular Biology Laboratory’ in Heidelberg. He became its first director, and held on to the post till 1981.

In 1981, after his retirement from the ‘European Molecular Biology Laboratory,’ Kendrew became the president of ‘St John's College’ at ‘Oxford University,’ a post which he held till 1987. Subsequently, he returned to Cambridge, where he was made an Honorary Fellow of ‘Trinity College’ and ‘Peterhouse.’

Kendrew is best remembered for his work on myoglobin. Since myoglobin is found in the muscle tissue of vertebrates, he first started working with horse’s heart, but later found that muscles from diving animals would be more suitable. Therefore, he procured whale meat from Peru and started working with it.

In 1957, using multiple isomorphous replacement (MIR) technique and X-ray analysis, he was able to develop a three-dimensional model of myoglobin molecule with 6A resolution. Not satisfied with the result, he continued with his work. In 1959, he was able to come up with a complete structure.

In 1962, Kendrew and Perutz jointly received the ‘Nobel Prize in Chemistry’ "for their studies of the structures of globular proteins." The same year, Kendrew was made a Companion of the British Empire.

 In 1965, he was awarded the ‘Royal Medal’ by the ‘Royal Society’ "in recognition of his distinguished contributions to the complete structural analysis of a protein molecule (myoglobin), particularly the biological aspects of this study."

In 1967, he became Fellow of the ‘American Society of Biological Chemists.’ He was also made an Honorary Member of the ‘International Academy of Science.’

Kendrew remained a bachelor for his whole life. He was also a very shy and private person. Music, history of art, and visiting places in Italy were among his hobbies.

After his retirement from ‘St John's College’ at ‘Oxford University,’ he returned to Cambridge. He died in Cambridge on 23 August 1997, at the age of 80.

On 16 October 2010, the ‘University of Oxford’ opened the ‘Kendrew Quadrangle’ at ‘St John's College’ in his honor.

The answering message on Kendrew’s phone was, "Please be patient and I shall get back to you as soon as possible."