Christian B. Anfinsen

Christian B. Anfinsen was an American biochemist whose experiments on ribonuclease showed that a protein’s amino acid sequence can determine its native structure. He shared the 1972 Nobel Prize in Chemistry.

Anfinsen's dogma: The principle that a protein’s amino acid sequence contains the information needed to determine its native structure under suitable conditions. This principle summarizes the conclusion Anfinsen drew from ribonuclease refolding.
Harvard University: A private research university in Cambridge, Massachusetts, founded in 1636. Anfinsen earned his doctorate in biochemistry there in 1943.
Stanford Moore: An American biochemist known for determining the chemical structure of ribonuclease with William H. Stein. Moore’s ribonuclease work helped establish the experimental foundation for Anfinsen’s folding studies.
Protein structure prediction: The computational and experimental effort to infer a protein’s three-dimensional structure from its sequence and other evidence. Anfinsen’s principle motivated attempts to derive structure directly from sequence.
Protein folding landscape: A representation of the possible conformations and energy states available to a folding protein. It frames how sequence can guide folding through many routes rather than one fixed path.
Ribonuclease A: A pancreatic enzyme that cleaves RNA and became a model protein in studies of folding and disulfide bonds. Anfinsen used this enzyme to test whether denatured proteins could recover their native form.
National Institutes of Health: The United States’ principal federal agency for biomedical and public health research. Anfinsen spent much of his career conducting research at the NIH.
William H. Stein: An American biochemist who developed methods for analyzing amino acid sequences and protein structure. Stein shared the 1972 chemistry Nobel Prize with Anfinsen and Moore for ribonuclease research.
Protein design: The creation or modification of amino acid sequences to produce proteins with chosen structures or functions. If sequence encodes structure, designing sequences offers a route to designing protein behavior.
Intrinsically disordered protein: A protein or protein region that lacks a single stable three-dimensional structure under ordinary physiological conditions. Such proteins challenge the idea that every sequence specifies one stable native shape.

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Kurt WüthrichRelated: Anfinsen's folding principle framed the biological significance of Wüthrich's structural measurements.