By Sanaa Mahmud, Research Team Member
Dorothy Hodgkin may not be a household name, but her contributions to the field of biochemistry remain crucial to many. If it were not for discoveries of the structures of insulin and penicillin, we would not have the same understanding of these drugs and their complex effects. Dorothy Hodgkin’s work remains very relevant to modern medicine as we continue to develop drug treatments for bacterial infections and diabetes.
Born as Dorothy Crowfoot in Cairo, Egypt, in 1910, she was introduced to a variety of subjects from a young age. Her father was part of the Egyptian Education Service and eventually moved to Sudan to work as the Director of Education and Antiquities. Her mother was involved in her father’s work and also pursued interests such as weaving, botany and drawing. As a child, Hodgkin became “captured for life by chemistry and by crystals”. According to her Nobel Prize biography, she was allowed to join the boys' chemistry class in school, which furthered her passion for science. When she moved to the UK, she also created her own lab in the attic, where she collected natural history artifacts and analyzed garden soil using a chemistry set given to her by a family friend.
In 1928, Hodgkin graduated from school and chose to pursue a degree in chemistry at Oxford University. She briefly combined her studies to include chemistry and archaeology, an interest most likely stemming from her father’s work, but Hodgkin ultimately chose to study chemistry and biochemistry. She also took special courses in crystallography, leading to her later research in X-ray crystallography. During her fourth year at Oxford, Hodgkin began a research project about the crystal structure of dimethyl thallium halides, a step that is said to have launched her career in crystallography.
After graduating from Oxford, Hodgkin went on to complete her PhD at Cambridge University. It was here that she was accepted into the lab of J.D. Bernal, an Irish scientist who was influential in using X-ray crystallography in molecular biology. Bernal’s groundbreaking photograph of the first X-ray of a protein crystal soon inspired Hodgkin to begin researching the 3D biochemical structure of insulin. Hodgkin graduated from Cambridge with a Ph.D. in crystallographic investigation of steroid crystals and became a university lecturer in addition to her research. Her investigations of biochemical structures became her life’s work.
Upon getting her Ph.D. and subsequent research fellowship and teaching positions, Hodgkin went to see a doctor about pain in her hands. She was diagnosed with a hand deformity called “ulnar deviation” caused by swelling in the knuckle joints. Nevertheless, Hodgkin continued in her research pursuits. In 1938, an infection triggered her first attack of rheumatoid arthritis. Hodgkin said she found it difficult to get up and get dressed, and “every joint in [her] body seemed to be affected.” Hodgkin returned to the lab after a few weeks of clinical treatment, but her hands did not allow her to use the main switch of the X-ray equipment. In a characteristic show of cleverness, she had a longer lever made for the switch and continued with her research.
It was not until WWII that Hodgkin began to study the structure of penicillin. In 1941, she became aware of a secret wartime effort to hone the use of antibiotics by establishing the structure of penicillin. Hodgkin wrote that she was “irresistibly drawn” to the project. At this time, biochemistry was still a novel field, and the three-dimensional structures of macromolecules were very unknown. Hodgkin worked with German-British biochemist Ernest Chain in developing a new technology to study biochemical structures, which involved crystallizing the molecules and then sending X-rays through them. The orbiting electrons in the atoms bent the x-rays into diffraction patterns, which could be captured on photographic plates in order to determine the structure of the molecule. Hodgkin and her research team eventually solved the structure of penicillin and built its first molecular model in 1945. She also used this incredible X-ray technique to discover the 3D structure of Vitamin B12 in 1954, and the 3D structure of insulin in 1969.
Hodgkin received the Nobel Prize in Chemistry in 1964 for the discovery of the structure of penicillin and other biochemical substances. She was the third woman to win a Nobel Prize, behind Marie Curie and Irene Joliot-Curie, and remains the only British woman to be awarded with a Nobel Prize in Chemistry. Despite her worsening arthritis, Hodgkin continued to teach and provide enthusiastic expertise around the world. She retired in 1988 and sadly died of a stroke in 1994 at the age of 84.
Dorothy Hodgkin is an incredible story of childhood passion turned into a lifetime of scientific discovery. Her work in X-ray crystallography not only contributed to our ability to understand the structures of insulin, penicillin, and vitamin B12, but also solidified X-ray crystallography as an essential tool. Without her contributions, the fields of biochemistry and medicine would be significantly less versed in the knowledge of effective treatments for diseases such as diabetes and anemia. Dorothy Hodgkin’s persistence in the face of arthritis continues to inspire scientists and young women in STEAM, showing that a strong passion for what you love can overcome any obstacle.