1910 - 1994 (84 years)
Has 2 ancestors and 3 descendants in this family tree.
||Dorothy Mary Crowfoot |
|Relationship||with Adam |
||12 May 1910
||29 Jul 1994
||Geneagraphie | Descendants of Francis Fox
||This person is also Dorothy Hodgkin at Wikipedia |
||5 Mar 2013 |
||Prof John Desmond Bernal, b. 10 May 1901, Nenagh, Co. Tipperary, Ireland , d. 15 Sep 1971, London, Middlesex, England (Age 70 years) |
||Type: a brief intimate relationship |
||5 Mar 2013 |
||Group Sheet | Family Chart
- British chemist and crystallographer, won the 1964 Nobel Prize in chemistry for X-ray studies of molecular compounds such as penicillin and vitamin B12.
During World War I (1914\endash 1918), Dorothy and her younger sisters lived in England, where they were cared for by their relatives and a nanny. As a child, Hodgkin traveled to locations in Africa and the Middle East with her parents. Dorothy attended the Sir John Leman School in Beccles, England.
For one of her birthdays. Crowfoot's mother gave her a book by the British physicist William Henry Bragg, a pioneer in the field of X-ray crystallography, which involves the use of X rays to study crystals. Crystals are solid substances that are composed of atoms arranged in planes, with regular spacing between the planes. When a beam of X rays is passed through the crystal, the planes act as tiny mirrors, diffracting (spreading out) the rays into a geometric pattern. Each type of crystal produces a different diffraction pattern. By capturing the pattern on film and then mathematically calculating the distances and relative positions of the individual spots in the pattern, Bragg and his son, William Lawrence Bragg, showed that it was possible to determine the precise geometric arrangement of atoms within different crystals. These two crystallographers (scientists specializing in crystallography) shared the 1915 Nobel Prize in physics for their work.
In 1928, Crowfoot entered Somerville College at Oxford University. Crowfoot received a bachelor's degree in chemistry in 1932.
After graduation from Somerville, Crowfoot got a job as an assistant to the well-known crystallographer John Desmond Bernal at Cambridge University. In 1934, Crowfoot and Bernal collaborated in determining the structure of the protein crystal pepsin. In 1934, she returned to Oxford to continue her doctoral studies and teach. Crowfoot regretted leaving Bernal, but her decision was a practical one: she needed the money, and the world economic depression of the 1930's had reduced the number of available jobs.
Working conditions at Oxford indeed posed a challenge for Crowfoot. She had to climb a rickety spiral staircase several times a day to reach the only window that let in enough light for her polarizing microscope to work. Although she was a member of the faculty, Crowfoot was not allowed to attend research meetings of the faculty chemistry club because she was a woman.
Crowfoot created a technique to determine the structure of cholesterol iodide, a sterol, which was the first complex organic material to be determined completely by X-ray crystallography. Using thousands of mathematical calculations, Hodgkin drew up a diagram of a cholesterol molecule showing the density of electrons struck by the X-ray beam. This density map indicated where atoms were located. She then created artificial crystals that were identical to natural ones except that they contained an extra atom of a heavy element. She compared X-ray photos of the artificial and natural crystals to fill in missing parts of the crystal's structure.
She received her doctoral degree from Cambridge in 1937 and continued to teach at Oxford for the rest of her career.
In 1937, Crowfoot married Thomas L. Hodgkin, a historian. Their jobs kept them apart during the week, but they spent weekends together. The couple had three children.
During World War II (1939\endash 1945), Dorothy Crowfoot Hodgkin joined a group of scientists attempting to determine the structure of penicillin, a powerful drug used to treat infections caused by bacteria. In 1945, Hodgkin and her colleagues succeeded.
After World War II, Hodgkin helped establish the International Union of Crystallography. She also joined several organizations working for world peace. Because some of these organizations admitted communists at a time when the American government opposed communism, Hodgkin was sometimes restricted in her travels to the United States.
In 1947, Hodgkin was elected a fellow (member) of the Royal Society, the leading scientific organization in the United Kingdom.
In 1948, Hodgkin began work to determine the structure of vitamin B12. Knowledge of the vitamin's molecular structure would help scientists better understand how the body uses this substance to build red blood cells and prevent a disease called pernicious anemia, which occurs when vitamin B12 cannot be absorbed by the body. This information would be useful to drug companies that wanted to produce a chemical form of vitamin B12 for people who could not get enough of the natural vitamin from their food.
Hodgkin set to work with a team of researchers. She also worked with Kenneth Trueblood, who led a group of American crystallogra-phers at the University of California in Los Angeles (UCLA). This group had access to a computer for help in the calculations. Hodgkin and Trueblood exchanged information by mail and telegraph. In 1957, they published the structure of vitamin B12.
Hodgkin's research on penicillin and vitamin B12 earned her the Nobel Prize in chemistry in 1964. In 1965, she became a member of the Order of Merit, one of Britain's highest awards. She was only the second woman to be honored with this award; the first had been the British nurse Florence Nightingale. She also received two awards from the Royal Society: the Royal Medal in 1956 and the Copley Medal in 1976.
Hodgkin next turned her research efforts toward insulin, a protein used to treat the disease diabetes. With 777 atoms, insulin had an extremely complex structure. With the aid of an improved computer, Hodgkin made the detailed calculations that allowed her to reveal the three-dimensional structure of insulin in 1969.
From 1960 to 1977, Hodgkin was the Royal Society Wolfson Research Professor at Oxford. In her later years, she traveled and participated in activities to promote world peace. In 1981, several colleagues edited a book in her honor called Structural Studies on Molecules of Biological Interest.
Hodgkin received the Mikhail Lomonosov Gold Medal of the Russian Academy of Sciences in 1982 and the Lenin Prize in 1987.