John C. Kendrew
Who was John C. Kendrew?
Nobel laureate: Nobel Prize in Chemistry (1962)
Biographical data adapted from Wikipedia’s article on John C. Kendrew (CC BY-SA 4.0).
Biography
Sir John Cowdery Kendrew was an English biochemist and crystallographer who made significant contributions to understanding protein structure through X-ray crystallography. Born in Oxford on March 24, 1917, he went to Dragon School, Clifton College, and Trinity College at the University of Cambridge. His scientific career was defined by his pioneering work at the Cavendish Laboratory, where he worked with Max Perutz to explore protein structures using crystallographic methods.
Kendrew's most notable scientific achievement was determining the atomic structure of myoglobin, a protein that stores oxygen in muscle tissue. This was the first time a protein structure was successfully identified at the atomic level, providing new insights into how proteins are built and work. This work involved years of detailed X-ray diffraction studies and complex math to interpret the data. His success with myoglobin helped start the field of structural biology and showed that protein structures could be solved experimentally.
Kendrew's research was internationally recognized when he shared the 1962 Nobel Prize in Chemistry with Max Perutz. He also received many other accolades, including Fellowship in the Royal Society, the Royal Medal in 1965, and a knighthood. He was named Commander of the Order of the British Empire and received the William Procter Prize for Scientific Achievement in 1988. He earned honorary doctorates and membership in prestigious scientific organizations as well.
Beyond his research, Kendrew played a significant role as a science administrator and educator. He helped set up key scientific institutions and served on various committees that influenced biological research in the post-war era. His work connected chemistry and biology at a time when combining these fields was vital for understanding life at the molecular level. Kendrew passed away in Cambridge on August 23, 1997, leaving a legacy that still impacts structural biology and biochemistry research worldwide.
Before Fame
John Kendrew's journey to becoming a prominent scientist began with his education at some of England's top schools during the time between the World Wars. After his studies at Dragon School and Clifton College, he went to Trinity College, Cambridge, where he was introduced to the new areas of biochemistry and molecular biology. The 1930s and 1940s were a time of big change for biological sciences, as scientists used physical and chemical methods to understand living systems in greater detail than ever before.
The development of X-ray crystallography as a tool for studying molecular structure opened up new possibilities for scientists like Kendrew to explore biological molecules. He entered this field just as experimental techniques and computational methods needed for interpreting complex diffraction patterns were advancing. The collaborative atmosphere at Cambridge, especially at the Cavendish Laboratory, was the perfect place for the interdisciplinary work that shaped his career.
Key Achievements
- First person to determine the complete three-dimensional atomic structure of a protein (myoglobin)
- Nobel Prize in Chemistry recipient (1962) shared with Max Perutz for protein structure determination
- Founded the field of structural biology through pioneering X-ray crystallography techniques
- Established myoglobin as the model system for understanding protein folding and oxygen storage
- Contributed to the development of computational methods for interpreting crystallographic data
Did You Know?
- 01.Kendrew's myoglobin structure determination required analyzing over 10,000 X-ray diffraction spots and took nearly two decades to complete
- 02.He was one of the founding members of the European Molecular Biology Organization (EMBO) in 1964
- 03.The myoglobin structure he solved contained 153 amino acids and was the first protein structure to reveal the characteristic alpha-helix folding pattern
- 04.Kendrew served as editor-in-chief of the Journal of Molecular Biology for many years, helping establish it as a leading publication in the field
- 05.His work required the use of some of the earliest computers for biological research, as the calculations were too complex for manual computation
Family & Personal Life
Awards & Honors
| Award | Year | Details |
|---|---|---|
| Nobel Prize in Chemistry | 1962 | for their studies of the structures of globular proteins |
| Fellow of the Royal Society | — | — |
| Commander of the Order of the British Empire | — | — |
| Royal Medal | 1965 | — |
| William Procter Prize for Scientific Achievement | 1988 | — |
| EMBO Membership | 1964 | — |
| honorary doctor of the University of Madrid Complutense | 1987 | — |
| Knight Bachelor | — | — |
| Honorary member of the British Biophysical Society | — | — |