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Stanford Moore

 

(born Sept. 4, 1913, Chicago, Ill., U.S. — died Aug. 23, 1982, New York, N.Y.) U.S. biochemist. He shared a 1972 Nobel Prize with Christian Anfinsen (1916 – 95) and William Stein (1911 – 80) for research on the molecular structures of proteins. He is best known for his applications of chromatography to the analysis of amino acids and peptides obtained from proteins and biological fluids and for the use of those analyses in determining the structure of the enzyme ribonuclease.

For more information on Stanford Moore, visit Britannica.com.

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Scientist: Stanford Moore
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American biochemist (1913–1982)

Moore, who was born in Chicago, Illinois, graduated in chemistry from Vanderbilt University in 1935 and received his PhD from the University of Wisconsin in 1938. He then joined the staff of the Rockefeller Institute, spending his entire career there and serving as professor of biochemistry from 1952 onward.

One of the major achievements of modern science has been the determination by Frederick Sanger in 1955 of the complete amino acid sequence of a protein. Sanger's success with the insulin molecule inspired Moore and his Rockefeller colleague, William Stein (1911–1980), to tackle the larger molecule of the enzyme ribonuclease. Although their work was lightened by the availability of techniques pioneered by Sanger the labor involved was still immense until eased by their development of the first automatic amino-acid analyzer.

They inserted a small amount of the amino-acid mixture into the top of a five-foot column containing resin. They then washed down the mixture using solutions of varying acidity. The individual amino acids travel down the column at different rates depending on their relative affinity for the solution and for the resin. It is possible to adjust the rates of travel so that the separate amino acids emerge from the bottom of the column at predetermined and well-spaced intervals. The colorless amino acids were then detected with ninhydrin, a reagent that forms a blue color on heating with proteins and amino acids. A continuous plot of the intensity of the blue color gives a series of peaks, each corresponding to a certain amino acid with the area under the peak indicating the amount of each.

By the end of the 1950s Moore and Stein had not only established the sequence of ribonuclease but they were also able to indicate the most likely active site on the single-chained molecule. For this work they shared the 1972 Nobel Prize for chemistry with Christian Anfinsen.

 
Columbia Encyclopedia: Stanford Moore
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Moore, Stanford, 1913-82, American biochemist, b. Chicago, Ph.D. Univ. of Wisconsin, Madison, 1938. Moore joined the faculty at the Rockefeller Institute for Medical Research (now Rockefeller Univ.) in New York in 1939 and remained there until his death in 1982. He received the 1972 Nobel Prize in Chemistry with Christian Anfinsen and William Stein for their work on the enzyme ribonuclease, which catalyzes the hydrolysis of RNA into smaller components. Moore and Stein are credited with describing in detail the chemical structure of catalytically active sites on the enzyme and their relation to the enzyme's biological activity.
(mʊr, môr), Stanford 1913–1982.

American biochemist. He shared a 1972 Nobel Prize for pioneering studies of the enzyme ribonuclease.

Wikipedia: Stanford Moore
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Stanford Moore
Born September 4, 1913
Died August 23, 1982
Nationality U.S.
Fields biochemistry
Institutions Rockefeller University
Alma mater Vanderbilt University, University of Wisconsin–Madison
Known for ribonuclease
Notable awards Nobel Prize in Chemistry in 1972

Stanford Moore (September 4, 1913 – August 23, 1982) was a U.S. biochemist. He won a Nobel Prize in Chemistry in 1972, for work he did at Rockefeller University on the structure of the enzyme ribonuclease and for contributing to the understanding of the connection between the chemical structure and catalytic activity of the ribonuclease molecule.

Moore attended Peabody Demonstration School, now known as University School of Nashville, and in 1935 graduated summa cum laude from Vanderbilt University, where he was a member of Phi Kappa Sigma. He earned his doctorate in Organic Chemistry from the University of Wisconsin–Madison in 1938. Moore then joined the staff of the Rockefeller Institute, later Rockefeller University, where he spent his entire professional career, with the exception of a period of government service during World War II. He became Professor of Biochemistry in 1952.

In 1958 he and William H. Stein developed the first automated amino acid analyzer, which facilitated the determination of protein sequences. In 1959 Moore and Stein announced the first determination of the complete amino acid sequence of an enzyme, ribonuclease, work which was cited in the Nobel award.

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