He shared the 1972 Nobel Prize in Chemistry with Stanford Moore and William Howard Stein for work on ribonuclease, especially concerning the connection between the amino acid sequence and the biologically active conformation (see Anfinsen's dogma).

[3] In 1939, he earned a master's degree in organic chemistry from the University of Pennsylvania and was awarded an American-Scandinavian Foundation 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 where he received his PhD in biochemistry in 1943.

[10][3] In 1962, Anfinsen returned to Harvard Medical School as a visiting professor and was invited to become chair of the department of chemistry.

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.