Generated by Llama 3.3-70B| John Kendrew | |
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| Name | John Kendrew |
| Birth date | March 24, 1917 |
| Birth place | Oxford, England |
| Death date | August 23, 1997 |
| Death place | Cambridge, England |
| Nationality | British |
| Fields | Biochemistry, Biophysics |
| Institutions | University of Cambridge, Royal Institution |
| Alma mater | Clifton College, University of Cambridge |
| Known for | Myoglobin structure |
| Awards | Nobel Prize in Chemistry |
John Kendrew was a renowned British biochemist and biophysicist who made significant contributions to the field of molecular biology. He is best known for determining the structure of myoglobin, a protein found in muscle tissue, using X-ray crystallography techniques developed by Max Perutz and Lawrence Bragg at the Cavendish Laboratory. Kendrew's work built upon the discoveries of Linus Pauling and Emil Fischer, and paved the way for future research in structural biology by scientists such as James Watson and Francis Crick.
Kendrew was born in Oxford, England, to a family of University of Oxford academics, and was educated at Clifton College in Bristol. He then went on to study chemistry at University of Cambridge, where he was heavily influenced by the work of Erwin Schrödinger and Niels Bohr. During his time at Cambridge, Kendrew became acquainted with Max Perutz, who would later become a close colleague and friend, and was also introduced to the work of Archibald Hill and Otto Warburg.
After completing his education, Kendrew worked at the Royal Institution in London, where he collaborated with William Lawrence Bragg and Henry Lipson on the development of X-ray crystallography techniques. He then moved to the Cavendish Laboratory at University of Cambridge, where he worked alongside Max Perutz and Francis Crick to determine the structure of myoglobin. Kendrew's work at Cambridge was also influenced by the research of Dorothy Hodgkin and Rosalind Franklin.
Kendrew's most notable achievement was the determination of the structure of myoglobin, which he accomplished using X-ray crystallography techniques. This discovery, which was published in the journal Nature in 1958, provided valuable insights into the structure and function of proteins and paved the way for future research in structural biology. Kendrew's work built upon the discoveries of Linus Pauling and Emil Fischer, and was influenced by the research of James Watson and Francis Crick on the structure of DNA. He also collaborated with Sydney Brenner and Matthew Meselson on the study of molecular biology.
Kendrew's contributions to biochemistry and biophysics were recognized with numerous awards and honors, including the Nobel Prize in Chemistry in 1962, which he shared with Max Perutz. He was also awarded the Copley Medal by the Royal Society in 1965, and was elected a Fellow of the Royal Society in 1960. Kendrew was also recognized by the American Academy of Arts and Sciences and the National Academy of Sciences.
Kendrew was known for his love of mountaineering and sailing, and was an avid traveler who visited many countries, including United States, Canada, and Australia. He was also a talented pianist and enjoyed playing the works of Ludwig van Beethoven and Wolfgang Amadeus Mozart. Kendrew was married to Elizabeth Jarvie, and had two children, Sarah Kendrew and Peter Kendrew. He passed away on August 23, 1997, in Cambridge, England, leaving behind a legacy of scientific discovery and innovation that continues to inspire researchers at institutions such as Harvard University, Stanford University, and Massachusetts Institute of Technology. Category:British biochemists