John Kendrew was an English biochemist and crystallographer who, along with Max Peutz, was one of the co-recipients of the 1962 Nobel Prize in Chemistry
@Crystallographer, Timeline and Personal Life
John Kendrew was an English biochemist and crystallographer who, along with Max Peutz, was one of the co-recipients of the 1962 Nobel Prize in Chemistry
John Kendrew born at
Kendrew was a life-long bachelor. He was also a very shy and private person with high artistic taste. Music, history of art and travelling through Italy were among his hobbies.
After his retirement from St John's College at Oxford University, he returned to live in Cambridge. Here, he died on 26 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 Oxford in his honor.
Sir John Cowdery Kendrew was born on 24 March 1917, in Oxford, U.K. His father, Wilford George Kendrew, was a reader in climatology in 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 was the norm those days. He passed out from there in 1936 and subsequently, received admission at Trinity College, Cambridge as a Major scholar.
In due course, he took 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 this event, the World War II broke out and Great Britain got involved in it.
John Kendrew spent first few months of the war doing research 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 as Telecommunications Research Establishment. Here he worked mainly on radar.
In 1946, on coming back to England, John Cowdery Kendrew approached Max Ferdinand Perutz. Perutz was a student of J. D. Bernal (whom Kendrew had met in Ceylon) and was working on structure of hemoglobin at the Cavendish Laboratory at that time.
Some time now, he also met Joseph Barcroft, an English physiologist, best known for his study on oxygenation of blood. Barcroft suggested that Kendrew might make a comparative protein crystallographic study of adult and fetal sheep hemoglobin.
Subsequently, Kendrew began his doctoral research under Perutz, who also taught him the elements of crystallography. Concurrently, they also began to work together under the direction of Sir Lawrence Bragg.
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 the Cavendish Laboratory under the guidance of Sir Lawrence Bragg. Subsequently, Kendrew became its Deputy Director and held the position till 1975.
Meanwhile, Kendrew and Perutz continued their work on the structure of sheep hemoglobin. Later, when the 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.
Kendrew is best remembered for his work on myoglobin. Since it is found in the muscle tissue of vertebrates he first started working with horse 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 isomorphic replacements technique and x-ray analysis, he was able to develop a three-dimensional model of the myoglobin molecule with 6A resolution. Not satisfied with the result, he continued with the work and in 1959, he was able to devise a more complete structure and show the arrangement of the amino acid units in it.