NIH News Release
National Library of Medicine

Thursday, November 2, 2000

Contact: Robert Mehnert
Kathy Cravedi
(301) 496-6308

Papers of Nobel Scientist Christian Anfinsen Added to "Profiles In Science" Web Site
Scientist Also Took Part in an International Rescue Mission in the Early 1980s

(Bethesda, Md.) — Most people do not think of Nobel Prize-winning scientists as embarking on dangerous international rescue missions. But in 1981, Nobel Laureate Christian Anfinsen traveled to Argentina to rescue 12 scientists detained as political prisoners by Jorge Rafael Videla, the military dictator who succeeded Juan Peron.

Christian Anfinsen (1916-1995) is the fifth scientist to be added to NLM's "Profiles in Science" website ( "Profiles in Science is now becoming a major online resource on which to store the public and private-and sometimes intimate-papers of this century's greatest biomedical scientists" says Dr. Donald Lindberg, director of the National Library of Medicine. "Christian Anfinsen joins Oswald Avery and fellow Nobelists Julius Axelrod, Joshua Lederberg, and Martin Rodbell."

Anfinsen, a biochemist at the National Institutes of Health from 1950 until 1981, was awarded the 1972 Nobel Prize in Chemistry for his work on the structure and composition of proteins in living cells. He also spent nearly a decade researching the protein interferon, which pharmaceutical companies have used to treat a variety of cancer- and AIDS-related illnesses.

"Less known, but certainly significant to Anfinsen's career, was his commitment to humanitarian and political issues, which he pursued with a vigor second only to that with which he pursued his laboratory work," said Dr. Alexa McCray, who directs the Profiles in Science project at the National Library of Medicine.

Christian Boehmer Anfinsen, Jr., was born to Norwegian immigrants on March 26, 1916 in Monessen, Pennsylvania, a small town south of Pittsburgh. He received a B.S. in chemistry from Swarthmore College in 1937, and his Ph.D. in biochemistry from Harvard in 1943. Anfinsen started teaching at Harvard, and while there worked for the federal government as a civilian biochemist, studying the metabolism of blood in both healthy monkeys and monkeys infected with malarial parasites.

In 1950, Anfinsen accepted a position at the National Institutes of Health. It was during this time that he became interested in the architecture of complex proteins called enzymes. Using an enzyme produced by the pancreas cells of cows, Anfinsen observed that the amino acids in the enzyme folded spontaneously into what Anfinsen later called the protein's "native conformation." By 1962, Anfinsen had developed his "thermodynamic hypothesis" of protein folding, which states that the native conformation is the most energy efficient form for a protein's shape to take. He then turned his attention to investigating an enzyme produced by the bacterium Staphylococcus aureus. By 1968, Anfinsen showed the complete structure of the enzyme by using affinity chromatography, an innovative laboratory technique.

Anfinsen's work in the late 1960s demonstrated that understanding the chemistry of proteins was essential to understanding the function of ribonucleic acid (RNA) in heredity. In order to prove that the structure of a protein determined its biological function, he artificially modified enzymes and then waited to see how their function was affected. Describing this work to an Israeli journalist in 1970, Anfinsen stated that "[W]e are engaged in what you may call molecular engineering. We look at the structure of an enzyme, for instance, and if we see a loop in the chain that doesn't seem to be doing anything, we see what happens if we chop it off."

After 1972, Anfinsen turned his attention to interferon, a protein generated by human cells that have been transformed by exposure to a virus, a parasite, or the actions of chemicals. Since the 1980s, drugs using purified forms of interferon have been used to treat multiple sclerosis, hepatitis C, leukemia, and AIDS-related Kaposi's sarcoma.

During the 1960s, Anfinsen divided his time between scientific work and political activism. He worked on the campaign that led to the 1963 treaty banning nuclear testing, and he joined other demonstrators on the NIH's campus who protested against the Vietnam War. After he won the Nobel prize Anfinsen used the considerable leverage of his Nobel Laureate status to champion other social concerns. In 1973, Anfinsen formed an alliance of NIH scientists and Nobel Laureates to protest Richard Nixon's budget cuts to biomedical research, and again in 1983 Anfinsen protested similarly austere budget cuts under Ronald Reagan's administration. From 1981 until 1989, Anfinsen served as chairperson of the National Academy of Sciences' Committee for Human Rights, during which time he and other committed scientists took their rescue mission to Argentina.

Anfinsen became increasingly uncomfortable with the potential misuses of biotechnology and genetic engineering in the 1980's. He believed that humanity could derive great benefits from biotechnology, but only with the right safeguards. In 1983, Anfinsen declared, "I sincerely believe that we can maintain adequate surveillance of the application of bioengineering to human beings so long as the human hunger for power and material gain does not become overwhelming."

The Christian Anfinsen website shows off a variety of documents and includes materials that span the various phases of Anfinsen's life and career. These include photographs, unpublished manuscripts, and a large sampling of his most important published articles, as well as correspondence documenting his commitments to various social and political causes.

"Profiles in Science" was launched September 1998 by the National Library of Medicine, a part of the National Institutes of Health in Bethesda, MD. It is a continuing project and the Library plans to announce each new collection as it is added to the site.

Note to editors: A photograph of Dr. Anfinsen is available from the NLM (email requests to