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Abstract
Father and son, William Henry Bragg and (William) Lawrence Bragg developed experimental methods and mathematical formulae that tell us how atoms are spatially configured in crystals of simple substances, as well as more complex macromolecules of living cells. In 1915, the Braggs were awarded the Nobel Prize in Physics for their work on X-ray crystallography, Lawrence being the youngest laureate at the time, being only 25 years of age.
William Bragg Senior was one of the motivators for Dorothy Hodgkin to use X-ray crystallography to examine the structures of biologically active substances. In part, this revolutionized modern medicine and improved health expectations. By advancing novel techniques of X-ray crystallography, she was able to elucidate the structures of numerous compounds, the most noteworthy of which were cholesterol, penicillin, vitamin B12 and insulin. Once Sanger had revealed the chemical structure of insulin, this led to its laboratory synthesis and improved treatments for diabetes – an autoimmune condition that was a major economic and health care burden. Hodgkin is the only British woman to have been awarded a Nobel prize (in 1964).
Lawrence Bragg inspired co-workers John Cowdery Kendrew and Max Perutz to use X-ray crystallography to determine the molecular structures of myoglobin and haemoglobin, physiologically important substances in binding molecular oxygen in animals. Myoglobin was the first protein to have its atomic structure determined by X-ray crystallography. For their research, Kendrew and Perutz shared the Nobel Prize in Chemistry, in 1962.
In the UK, with about 1% of the Earth’s population, ‘Bioscience Britain’ has been responsible for major advances in identifying the circulation of blood; smallpox vaccination; evolution; penicillin; X-ray crystallography of biologically active substances; amino acid and nucleotide sequencing; in-vitro fertilisation; structure of, and fingerprinting by, DNA; cloning and genome sequencing.
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