| Christian B. Anfinsen | |
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Christian B. Anfinsen in 1969
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| Born | Christian Boehmer Anfinsen, Jr. March 26, 1916 Monessen, Pennsylvania |
| Died | 14 May 1995 (aged 79) Randallstown, Maryland |
| Nationality | American |
| Fields | Biochemistry |
| Alma mater | Swarthmore College (BS, 1937) University of Pennsylvania (MS, 1939) Harvard Medical School (PhD, 1943) |
| Known for | Ribonuclease, Anfinsen's dogma |
| Notable awards | Nobel Prize in Chemistry (1972) |
Christian Boehmer Anfinsen, Jr. (March 26, 1916 – May 14, 1995) was an American biochemist. He shared the 1972 Nobel Prize in Chemistry with Stanford Moore and William Howard Stein for work on ribonuclease, especially concerning the connection between the amino acid sequence and the biologically active conformation (see Anfinsen's dogma).[1]
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Christian Anfinsen was born in Monessen, Pennsylvania into a family of Norwegian American immigrants. The family moved to Philadelphia in the 1920s. He earned a bachelor's degree from Swarthmore College in 1937. While attending Swarthmore College he played varsity football and joined the Delta Upsilon Fraternity.
In 1939, he earned a master's degree in organic chemistry from the University of Pennsylvania. In 1939, The American-Scandinavian Foundation awarded Anfinsen a fellowship to develop new methods for analyzing the chemical structure of complex proteins, namely enzymes, at the Carlsberg Laboratory in Copenhagen, Denmark. In 1941, Anfinsen was offered a university fellowship for doctoral study in the Department of Biological Chemistry at Harvard Medical School. Anfinsen received his Ph.D. in biochemistry in 1943 from Harvard Medical School.[2] He converted to Judaism by undergoing an Orthodox conversion in 1979. In the same year he also quit smoking.[3]
In 1950, the National Heart Institute, part of the National Institutes of Health in Bethesda, Maryland, recruited Anfinsen as chief of its Laboratory of Cell physiology. In 1954, a Rockefeller Foundation fellowship enabled Anfinsen to return to the Carlsberg Laboratory for a year and a Guggenheim Foundation fellowship allowed him to study at the Weizmann Institute of Science in Rehovot, Israel from 1958–59.[4] He was elected a Fellow of the American Academy of Arts and Sciences in 1958.[5]
In 1962, Anfinsen returned to Harvard Medical School as a visiting professor and was invited to become chair of the Department of Chemistry. He was subsequently appointed Chief of the Laboratory of Chemical Biology at the National Institute of Arthritis and Metabolic Diseases (now the National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases), where he remained until 1981. From 1982 until his death in 1995, Anfinsen was Professor of Biophysical Chemistry at Johns Hopkins.[6]
Anfinsen published more than 200 original articles, mostly in the area of the relationships between structure and function in proteins. He was also a pioneer of ideas in the area of nucleic acid compaction. In 1961 he showed that ribonuclease could be refolded after denaturation while preserving enzyme activity, thereby suggesting that all the information required by protein to adopt its final conformation is encoded in its primary structure. He belonged to the National Academy of Sciences (USA), the Royal Danish Academy of Sciences and Letters and the American Philosophical Society.[3][7]
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