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Examples
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In addition to his research activities, Dr. Anfinsen is an editor of Advances in Protein Chemistry, served on the Editorial
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Anfinsen had shown, with the enzyme ribonuclease, that the information for a protein assuming a specific three-dimensional structure is inherent in its amino-acid sequence, and this discovery was the starting point for studies of the mechanism of protein folding, one of the major areas of present-day biochemical research.
The Nobel Prize in Chemistry: The Development of Modern Chemistry 2010
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B. Anfinsen of NIH and the other half shared by Stanford
The Nobel Prize in Chemistry: The Development of Modern Chemistry 2010
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You'll see Nobel Laureate Anfinsen (also from JHU) giving an endorsement for Spetners book on the back cover!
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It was an occasion for me to get together with my friends on the East Coast: Herb and Eva Sober and Chris and Flossie Anfinsen from NIH, Bill and Inge
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Christian B. Anfinsen, William H. Stein, and I have the honor of co-authoring the response of three chemists to your toast on this memorable occasion.
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In recent years, Anfinsen has devoted himself primarily to comprehensive investigations of an extracellular nuclease of
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In the mid 1950's Anfinsen began to concentrate on the problem of the relationship between structure and function in enzymes.
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Anfinsen has shown that this information is inherent in the linear sequence of amino acid residues in the peptide chain, so that no further genetic information than that found in DNA is needed.
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Ribonuclease was the first enzyme for which the complete amino acid sequence was determined thanks to contributions from Anfinsen and from Moore and Stein.
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