This Biography is about one of the best Biochemist Christian Anfinsen including his Height, weight, Age & Other Detail…
Biography Of Christian Anfinsen | |
Real Name | Christian Anfinsen |
Profession | Biochemists |
Famous as | Biochemist |
Nationality | American |
Personal life of Christian Anfinsen | |
Born on | 26 March 1916 |
Birthday | 26th March |
Died At Age | 79 |
Sun Sign | Aries |
Born in | Monessen, Pennsylvania |
Died on | 14 May 1995 |
Place of death | Randallstown, Maryland |
Family Background of Christian Anfinsen | |
Father | Christian Boehmer Anfinsen, Sr |
Mother | Sophie Rasmussen Anfinsen |
Spouses/Partners | Florence Bernice Kenenger, Libby Esther Shulman Ely |
Children | Carol, Margot, Christian, Mark, Tobie, Daniel, David |
Education | Swarthmore College (BA, 1937), University of Pennsylvania (MS, 1939), Harvard Medical School (PhD, 1943) |
Awards | Nobel Prize in Chemistry (1972) |
Personal Fact of Christian Anfinsen | |
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. |
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