Dorothy Crowfoot-hodgkin

Picture of Dorothy Crowfoot-hodgkin

Date of Birth: 05/12/1910

Age: 84

Place of birth: Cairo

Citizenship: United Kingdom


When the First World War, his parents sent children to England, to his grandmother on his father`s side in Worthing town, a few miles from Brighton on the English Channel. After the cessation of hostilities in 1918 his mother, Dorothy returned to England and settled with their children in Lincoln, where in the home to teach them the history, science and literature. Over the next three years the mother shuttled between England and the Middle East, has not yet settled in the city Geldstone, East Suffolk, where Crowfoot ancestors lived for centuries.

Until 1928 Crowfoot attended John Lyman School, located near Beckles. In school, she was fascinated with crystals, and this led her to the study of crystallography and chemistry. At the age of 13, she visited her father in Khartoum and here performed a quantitative analysis of some of the local minerals supervised A.F.Dzhozefa (AFJoseph), chemist and soil scientist.

In 1926 my father became the director of the British School of Archaeology in Jerusalem, and after graduation Crowfoot comes to his parents to Palestine. Digging Byzantine churches in Jerash (Jordan), she was fascinated by archeology, but when he returned to England, began to study chemistry at Somerville College, Oxford. By combining their knowledge in the field of botany and archeology, she decided to apply lessons from its parent methods of these sciences to chemical research.

Crowfoot first learned about the X-ray diffraction in crystals from the book On the Nature of Things, written by William Henry Bragg (Nobel Laureate in Physics, 1915) for schoolchildren. She studied crystallography under the direction of X.M.Pouella (HMPowel) in Somerville. Summer spent the summer in Heidelberg at the laboratory of Victor Goldschmidt (Victor Goldschmidt, 1853-1933), another specialist in this field.

After graduating from Somerville College in 1932 Crowfoot received a small stipend, which, together with financial support from the aunt allowed her to work at Cambridge University with outstanding physicist John Desmond Bernal (John Desmond Bernal, 1901-1971). Bernal then analyzed the steroid molecules. Her collaboration with Bernal led to decisive advances in the first stage of studies in the field of X-ray analysis of crystals of globular proteins. This period starts from their success in 1934, when they developed a method for analysis of single crystals of the protein, immersed in the mother liquor.

In 1935 Crowfoot returned to Oxford, where she was first a mentor. Received via R.Robinsona (Nobel Laureate, 1947), a subsidy for the purchase of X-ray apparatus, Crowfoot took yodholesterina analysis. For this work, which, according to U.G.Bregga, is an example of the use of physical method to determining the complex spatial structures in organic chemistry, in 1937, she received her doctorate. Bernal wrote: "Her success made her old professor Sir Robert Robinson say that now about the structure of molecules much more can be found on the basis of X-ray analysis, and chemists have to do their work - synthesis of substances."

In 1937 Crowfoot married L.Hodzhkina Thomas (Thomas L.Hodgkin), son of an Oxford historian, a descendant of the physician Thomas Hodgkin (Thomas Hodgkin, 1798-1866), which is named in honor of Hodgkin`s disease (limfogranulomatoz).

Three years after the Second World War Crowfoot Hodgkin began to study penicillin and successfully solved it in 1949, to determine the molecular structure of the antibiotic.

In 1948, she applied for the study of X-ray analysis of vitamin B12 and finally identified the molecular structure of this complex in the structure of the substance in 1956

In 1956 he became a lecturer at the rate of X-ray crystallography. In 1958 it moved from laboratory scattered in different locations of rooms in the University Museum of Natural History - a modern building, built to meet the requirements of chemical science.

Crowfoot Hodgkin received the Nobel Prize in 1964 "for the determination by X-ray structures of biologically active substances."

Then she went on it started back in the 1930s, studies of insulin and in 1972 graduated from the analysis of Zn-insulin. Work on this complex molecular structure, which contains nearly 800 atoms (vitamin B12 consists of 90 atoms) has been further complicated by the fact that insulin is crystallized to form a plurality of forms. Then Crowfoot Hodgkin figured out the role of vitamin B12 in the body and modifikatsirovala its molecules to alter the physiological properties. She has been studied lactoglobulin, pepsin, hemoglobin, vegetable globulins.

Between 1960 and 1977 she served as a professor and researcher of the Royal Society. From 1977 to 1982 - Member of the Board of Wolfson College at Oxford. Honorary Rector (1970-1988) at Bristol University, and since 1975 - the president of the Pugwash movement.

Crowfoot Hodgkin remained active lab employee, stating: "There is still a lot of complex crystals, which challenge us."

Works: X-ray analysis of the structure of penicillin // Advancement Sci. 1949. V. 6; X-ray crystallographic study of the structure of vitamin B12 // Bull. Soc. Franc. Mineral et Cryst. 1955. V. 78. P. 106-115; Structural Studies on Molecules of Biological Interest. New York, 1981.