Christian Anfinsen

Biography

Christian Boehmer Anfinsen Jr. was born on March 26, 1916, in Monessen, Pennsylvania. His father, Christian Boehmer Anfinsen Sr., was a Norwegian immigrant who worked as a machinist, and his mother was Sophie Rasmussen Anfinsen. After graduating from Monessen High School, Anfinsen went to Swarthmore College, where he earned a bachelor's degree in chemistry in 1937. He then attended the University of Pennsylvania, receiving his master's degree in organic chemistry in 1939, and pursued a Ph.D. in biochemistry at Harvard Medical School, completing it in 1943.

Anfinsen's career began at several top institutions. He was a research associate at the Carnegie Institution of Washington and later joined Harvard Medical School as an assistant professor. In 1950, he moved to the National Institute of Arthritis and Metabolic Diseases at the National Institutes of Health, where he conducted his most influential research. During a sabbatical in the mid-1950s, supported by a Guggenheim Fellowship, he worked with Kaj Linderstrøm-Lang at the Carlsberg Laboratory in Copenhagen, Denmark, gaining expertise in protein chemistry techniques.

Anfinsen's major scientific breakthrough was his work on ribonuclease, a protein enzyme that breaks down RNA. He showed that a protein's amino acid sequence determines its shape, which in turn determines its function. His experiments revealed that when ribonuclease was unfolded and then refolded under the right conditions, it returned to its original structure and activity. This finding, known as Anfinsen's dogma or principle, revolutionized the understanding of protein folding and structure.

For this important work, Anfinsen shared the 1972 Nobel Prize in Chemistry with Stanford Moore and William Howard Stein, who had done related research on ribonuclease. His research laid the groundwork for modern protein science and helped in understanding diseases caused by protein misfolding. Later, Anfinsen explored the origin of life and evolution, researching how proteins might have evolved from simpler peptides. He passed away on May 14, 1995, in Randallstown, Maryland, leaving a legacy that continues to impact biochemistry and molecular biology research around the world.