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 was a convert to Judaism by going through the gijur_process.
Dr. Anfinsen obtained a B.A. degree from Swarthmore College in 1937 and an M.S. in organic chemistry in 1939 from the University of Pennsylvania.
Anfinsen left Harvard in 1950 to become Chief of the Laboratory of Cellular Physiology and Metaolism in the National Heart Institute of the National Institutes of Health.
In Anfinsen's early work, he and Steinberg studied the non-uniform labelling in newly synthesized proteins - a technique with later permitted Dintzis, Canfield and others to determine that proteins are synthesized sequentially from the amino-terminal and in vivo, and to calculate the rate at which amino acids are polymerized.
Christian Boehmer Anfinsen was born in Monessen, Pennsylvania, on March 26, 1916.
Anfinsen demonstrated that the denaturation of the enzyme was reversible.
Although Anfinsen could not have known the importance of his discoveries in the 1960s, he was somewhat concerned that the breaking of the genetic code and discovery of the α-helix structure of DNA overshadowed the work on protein and enzyme structure and function.
Feeds |
Contact