Research Kept Anfinsen Busy In Later Years By Emil Venere and Ken Keatley / Office of News and Information Christian Anfinsen talked about possibly retiring when he turned 80. But, at 79, the legendary biochemist was doing important research on bacteria that thrive in the ultra-hot waters along volcanic vents on the ocean floors. One of his goals was to isolate enzymes that might be used to neutralize the world's dangerous stockpiles of chemical weapons. Biology professor Evangelos Moudrianakis, a longtime friend, said the Nobel laureate was perhaps involved in the most significant work of his career--understanding how these enzymes function. There was another side to Anfinsen. A side that belied his scientific prowess, said Moudrianakis and other colleagues. "Everything he did was inspiring, but he did it in a very, very low key, mild-mannered way," said biology professor Philip Hartman. "You'd never know he was a Nobel Prize winner. He was as modest as you can get. "He remarked to me recently that maybe he should retire and make way for young investigators. He was always concerned with young people." That's the last image his colleagues have of Anfinsen--a hard-working, compassionate man of science who cared more about the implications of his actions than his own reputation. On Sunday, May 14, he suffered an apparent heart attack at his Pikesville home and was later pronounced dead at Northwest Hospital Center in Randallstown. Anfinsen won the 1972 Nobel Prize in chemistry and joined the Hopkins faculty in biology in 1982. "He was obviously a very major scientific talent but also a very warm and wonderful person," said former Hopkins president Steven Muller, who appointed Anfinsen. "I thought the world of him." He won the Nobel Prize while chief of the laboratory of chemical biology at what is now known as the National Institute of Arthritis, Metabolism and Digestive Diseases. He shared the prize with Rockefeller University scientists Stanford Moore and William H. Stein; they were honored for their clarification of the relationship between the structural properties of proteins and their biological functions. Specifically, Anfinsen helped to discover how the protein enzyme ribonuclease folds to obtain the characteristic three-dimensional structure that determines its function. "Dr. Anfinsen was a true pioneer in the field of protein structure and protein folding," said Daniel Nathans, a Nobel Prize-winning physician and molecular biologist at Hopkins who will become the university's interim president June 1. "His work is the prototype for the many studies that have followed, and the work still being done in this area." A native of Monessen, Pa., Anfinsen earned his bachelor of arts degree in 1937 from Swarthmore College and his master's degree in organic chemistry in 1939 from the University of Pennsylvania. In 1943, he received a doctorate in biochemistry from Harvard Medical School, where he was an instructor and assistant professor of biological chemistry from 1943 to 1950. While at Harvard, he spent a year as senior fellow of the American Cancer Society, working with Hugo Theorell at the Medical Nobel Institute in Sweden. Anfinsen joined the National Institutes of Health in 1950 as chief of the Laboratory of Cellular Physiology and Metabolism in the National Heart Institute. From 1963 to 1981, he was chief of the Laboratory of Chemical Biology in the National Institute of Arthritis and Metabolic Diseases. Upon retirement from NIH in 1981, he spent a year in residence at the Weizmann Institute of Science in Rehovot, Israel, before coming to Hopkins. He often joined forces with other scientists in calling for the responsible use of research and to discourage the development of biological weapons. In 1988, as a member of the Committee for Responsible Genetics, he urged Congress not to fund a $300 million request by the Department of Defense for biological weapons research. He is survived by his wife, Libby; a sister; two daughters; a son; four stepchildren; and 13 grandchildren. The family requested that any memorial contributions be made to the American Committee for the Weizmann Institute of Science, 51 Madison Ave., New York, N.Y., 10010.
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