The 1972 Nobel Prize in Chemistry was shared by Christian B. Anfinsen, Stanford Moore, and William Howard Stein for their investigation into ribonuclease. Anfinsen’s specific contribution centered on the correlation between an amino acid sequence and the biologically active conformation of proteins, a principle that became foundational to the study of molecular biology and protein folding.
Early Education and Research
Born in Monessen, Pennsylvania, in 1916, Anfinsen attended Monessen High School before enrolling at Swarthmore College in 1933. He earned a bachelor's degree in chemistry in 1937 and participated in varsity football. By 1939, he completed a master's degree in organic chemistry at the University of Pennsylvania. An American-Scandinavian Foundation fellowship then supported his work at the Carlsberg Laboratory in Copenhagen, Denmark, where he began developing techniques for protein analysis. He obtained his PhD in biochemistry from Harvard Medical School in 1943.
Twenty questions, eight minutes on the clock, and a percentile measured against everyone who has taken it. No sign-up.
Take the IQ test →Academic and Institutional Roles
During World War II, Anfinsen served at the Office of Scientific Research and Development. In 1950, he joined the National Heart Institute as chief of its laboratory of cell physiology. His career included international research stints, specifically at the Carlsberg Laboratory and the Weizmann Institute of Science in Rehovot, Israel. He served as a visiting professor at Harvard Medical School in 1962 and later acted as chief of the laboratory of chemical biology at the National Institute of Arthritis and Metabolic Diseases until 1981. He finished his career as a Professor of Biology and Biochemistry at Johns Hopkins University, a position held from 1982 until his death in 1995.
Contributions to Biochemistry
Anfinsen authored over 200 original articles and the 1959 book, The Molecular Basis of Evolution, which examined the intersection of protein chemistry and genetics. In 1961, his experiments demonstrated that ribonuclease could be refolded after denaturation while maintaining its enzymatic activity. This observation suggested that a protein’s final conformation is dictated by its amino acid sequence. Beyond his research, he was a founding member of the World Cultural Council and held memberships in the National Academy of Sciences, the American Philosophical Society, and the Pontifical Academy of Sciences.
Fast facts
- Born: 1916, Monessen, Pennsylvania
- Died: 1995, Randallstown, Maryland
- Education: Swarthmore College, University of Pennsylvania, Harvard Medical School
- Nobel Prize: 1972, Chemistry
- Major work: The Molecular Basis of Evolution (1959)
- Professional appointments: Harvard University, Johns Hopkins University
- Burial location: Beth Tfiloh Cemetery
Questions readers ask
What is Anfinsen's dogma?
It is the principle that the native structure of a protein is determined by the totality of its amino acid sequence under physiological conditions.
What did Anfinsen study at the Carlsberg Laboratory?
He developed methods for analyzing the chemical structure of complex proteins, specifically enzymes.
.jpg)