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Dorothy Hodgkin

Dorothy Crowfoot Hodgkin was awarded the Nobel Prize in Chemistry 1964 "for her determinations by X-ray techniques of the structures of important biochemical substances" (Image: Copyright © The Nobel Foundation/Wikimedia Commons)

Dorothy Crowfoot Hodgkin was awarded the Nobel Prize in Chemistry 1964“for her determinations by X-ray techniques of the structures of important biochemical substances” (Image: Copyright © The Nobel Foundat... moreion/Wikimedia Commons)

Oxford housewife wins Nobel” ran the headline of British newspaper The Daily Mail when Dorothy Hodgkin won the Nobel Prize in 1964. Hardly a fitting tribute for one of her generation’s finest intellects, but an important milestone for both science and the women who are scientists.

Dorothy Crowfoot Hodgkin (1910 – 1994) was a British biochemist best known for developing the area of protein crystallography, using a technique that employs x-rays to examine the pattern of atoms inside organized materials. At first sight one might think this would be restricted to substances such as quartz or rock-salt, but although not strictly crystalline the deep structure of proteins can also be understood using this technique.

Elected a Fellow of the Royal Society in 1947, almost thirty years later (in 1976) she was awarded the most prestigious honour the Society can confer, the Copley Medal. This was, to quote, “in recognition of her outstanding work on the structures of complex molecules, particularly Penicillin, vitamin B12 and insulin” (Royal Society). Winning this medal is perhaps less surprising when we recall that it was Hodgkin’s work on vitamin B12 that led to her being awarded the Nobel Prize in 1964, while in 1965 she became the second woman (the first being Florence Nightingale) to receive the Order of Merit.

It is possible that had chemistry not captured Hodgkin’s childhood imagination as completely as it did (by the age of 12 she was carrying out her own chemical experiments in the attic of her family home), she may well have pursued a life in archaeology. Hodgkin came from a distinguished family of archaeologists. Her father John Winter Crowfoot was appointed Director of the British School of Archaeology in Jerusalem in 1926, carrying out a series of notable excavations which included the Hill of Ophel in Jerusalem in 1927, and Samaria-Sebaste in 1931-1935. Her youngest sister, Diana Crowfoot Rowley, would go on to work on the archaeology and geology of the Canadian Arctic.

Nevertheless, her parents encouraged an interest in chemistry and in 1928 Hodgkin went up to Oxford to read chemistry. It is a testimony, however, to Hodgkin’s endlessly inquisitive mind that she maintained an interest and skill in various aspects of archaeology. She took part in a number of her father’s excavations, which included sketching ancient mosaics and subsequently analysing the glass collected from these sites in her laboratory in the University Museum at Oxford. As a point of interest, the room in which Hodgkin worked was the same place where, in 1860 at a meeting of the British Association for the Advancement of Science, the biologist Thomas Henry Huxley and Bishop Samuel Wilberforce held their now famous debate about evolution (Glusker 1994).

It was, however, protein crystallography to which Hodgkin would dedicate her academic life. Modern crystallography has its roots in 1895, when the physicist Wilhelm Conrad Röntgen discovered a new form of electromagnetic radiation. X-rays changed the way we would view the world (and the Universe) by changing the way we were able to view it, a revolutionary technique that would have profound ramifications for healthcare, and also enable us to peer deep into the structure of matter itself. First called Röntgen radiation, this part of electromagnetic spectrum is now known as x-rays.

The discovery of x-rays in 1895 by the German physicist Wilhelm Conrad Röntgen changed the way we viewed the world – and the Universe. It provided us with a new tool to peer inside the structure of matter itself, bringing huge benefits across the scientific world, from medicine to astronomy, and laying the foundation for modern (Image: NASA/JPL-Caltech/GSFC)

The discovery of x-rays in 1895 by the German physicist Wilhelm Conrad Röntgen changed the way we viewed the world (and the Universe). It provided us with a new tool to peer inside the structure of matter itself, bring... moreing huge benefits across the scientific world, from medicine to astronomy, and laying the foundation for modern crystallography. This image shows x-rays streaming off the sun as captured by NASA’s Nuclear Spectroscopic Telescope Array (Image: NASA/JPL-Caltech/GSFC)

By aiming x-rays at a crystal and noting the particular directions it caused the x-rays to diffract, crystallographers (pioneered by physicists William Henry Bragg and his son William Lawrence Bragg) were able to build up a three dimensional understanding of how atoms were arranged in certain types of matter. At first, x-ray crystallography could only be used to study solid crystals with a lattice of regularly arranged atoms. By the late 1950s, and thanks to the work of scientists such as Sir John Cowdery Kendrew, it was realised that by making crystals out of biological materials such as proteins, the technique could also be applied to fields relevant to both biology and medicine.

In 1932 Hodgkin was awarded a first class honours degree from Oxford and subsequently began to study for a PhD at the University of Cambridge with the highly influential (and sometimes controversial) crystallographer John Desmond Bernal. In 1934 Hodgkin and Bernal became the first scientists to take an x-ray photograph of a protein structure, specifically a pepsin. Not only did this pave the way for protein crystallography, but it also heralded the beginning of structural molecular biology. Hodgkin subsequently described the structures of cholesterol (1941), penicillin (1945), vitamin B12 (1956), and insulin (1969). Hodgkin’s work on insulin, penicillin, and vitamin B12 had immense medical implications. The early accomplishments are all the more remarkable when one considers that in the 1930s there were no computers to aid in the complicated analyses, so that all the calculations had to be carried out by hand.

X-ray crystallography is a highly interdisciplinary science, linking physics, biology, and chemistry. Directly and indirectly it has produced the largest number of Nobel Laureates for any scientific field. Apart from Hodgkin here are just the names mentioned in this article: Wilhelm Conrad Röntgen earned the Nobel Prize in Physics in 1901; William and Lawrence Bragg shared the Nobel Prize for physics in 1962; John Cowdery Kendrew and Max Perutz shared the 1962 Nobel Prize for chemistry.

Hodgkin was also a notable humanitarian. From 1976 to 1988 she was president of the Pugwash Conferences on Science and World Affairs, an international organization that aims to bring together key public figures and academics in an attempt to diminish conflict, and in 1985 she was awarded the Soviet Union’s Lenin Peace Prize.

We leave the final words to one of Hodgkin’s long term collaborators, the molecular biologist Max Perutz (2011):

She will be remembered as a great chemist, a saintly, gentle and tolerant lover of people and a devoted protagonist of peace.

Text copyright © 2015 Victoria Ling. All rights reserved.

References
Dodson, G. 2002. Dorothy Mary Crowfoot Hodgkin, O.M. 12 May 1910 – 29 July 1994. Biographical Memoirs of the Royal Society 48, 179-212.
Ferry, G. 2014. Dorothy Hodgkin: A life. Bloomsbury.
Glusker, J. P. 1994. Dorothy Crowfoot Hodgkin (1910-1994). Protein Science 3, 2465–2469.
Howard, J. A. K. 2003. Timeline: Dorothy Hodgkin and her contributions to biochemistry. Nature Reviews Molecular Cell Biology 4, 891–896.
Perutz, M. 2011. Obituary: Professor Dorothy Hodgkin. The Independent (18.11.2011).
Royal Society. Award winners: Copley Medal.

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