Christian Anfinsen

About Christian Anfinsen

Who is it?: Biochemist
Birth Day: March 26, 1916
Birth Place: Monessen, Pennsylvania, United States
Died On: May 14, 1995(1995-05-14) (aged 79)\nRandallstown, Maryland
Birth Sign: Aries
Alma mater: Swarthmore College (BA, 1937) University of Pennsylvania (MS, 1939) Harvard Medical School (PhD, 1943)
Known for: Ribonuclease, Anfinsen's dogma
Spouse(s): Florence Kenenger (1941-1978; divorced; 3 children) Libby Shulman Ely (m. 1979; 4 stepchildren)
Awards: Nobel Prize in Chemistry (1972)
Fields: Biochemistry

Christian Anfinsen Net Worth

Christian Anfinsen was bornon March 26, 1916 in Monessen, Pennsylvania, United States, is Biochemist. Christian Boehmer Anfinsen was an American biochemist who won the Nobel Prize for his pioneering work on the structure of enzymes and the relationship between enzyme functions and the amino acid sequence. He shared the prize with two other American scientists, William Howard Stein and Stanford Moore. From his experiments on the ‘ribonuclease’ enzyme he came to the conclusion that the information regarding the tertiary structure of the enzyme is contained in the sequential structure of the amino acids present along the protein chain. His work led to the understanding of the causes of many diseases such as Alzheimer’s disease, mad cow disease, cystic fibrosis, genetic emphysema and many types of cancers. His early work with Steinberg was on the non-uniform labeling of newly synthesized proteins which later helped Canfield and Dintzis to determine that proteins are sequentially synthesized from amino acids ‘in vivo’ and to find out the rate of polymerization of amino acids. In the mid-1950s Anfinsen concentrated on the structure and function of enzymes which helped him suggest the ‘thermodynamic hypothesis’ related to the refolding of many proteins to their native forms even after the cleavage of the disulphide bonds which disrupted the tertiary structure.
Christian Anfinsen is a member of Scientists

💰 Net worth: Under Review

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Biography/Timeline

1920

Anfinsen was born in Monessen, Pennsylvania, into a family of Norwegian American immigrants. His parents were Sophie (née Rasmussen) and Christian Boehmer Anfinsen Sr., a mechanical Engineer. 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.

1939

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. There, Anfinsen received his Ph.D. in biochemistry in 1943. In 1979, he converted to Judaism, by undergoing an Orthodox conversion and that same year he quit smoking. Although Anfinsen wrote in 1985 that his feelings on religion still reflect a fifty-year period of orthodox agnosticism.

1941

Anfinsen had three children with his first wife, Florence Kenenger, to whom he was married from 1941 to 1978. He married Libby Shulman Ely, with whom he had 4 stepchildren, in 1979.

1950

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. He was elected a Fellow of the American Academy of Arts and Sciences in 1958.

1961

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 amino-acid sequence. He belonged to the National Academy of Sciences (USA), the Royal Danish Academy of Sciences and Letters and the American Philosophical Society.

1962

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. In 1981, Anfinsen became a founding member of the World Cultural Council. From 1982 until his death in 1995, Anfinsen was Professor of Biophysical Chemistry at Johns Hopkins.

1996

Established in 1996, The Christian B. Anfinsen Award is presented annually to distinguished Scientists, the Awards recognize excellence and outstanding achievements in the multidisciplinary fields of protein science, and honor distinguished contributions in the areas of leadership, education, or Service. It is sponsored by The Protein Society, and recognizes significant technical achievements in the field of protein science.

1998

His papers were donated to the National Library of Medicine by Libby Anfinsen between 1998 and 1999.