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World of Scientific Discovery on Stanford Moore
Stanford Moore was born in 1913, in Chicago, Illinois, but spent most of his childhood in Nashville, Tennessee, where his father was a professor at Vanderbilt University's School of Law. In 1935 Moore earned a B.A. in chemistry from Vanderbilt. Moore attended graduate school at the University of Wisconsin and completed a Ph.D in organic chemistry in 1938. He accepted a position in 1939 as a research assistant in the laboratory of German chemist Max Bergmann at the Rockefeller Institute for Medical Research (RIMR), later renamed Rockefeller University.
Bergmann's research group focused on the structural chemistry of proteins. During his early years at RIMR, Moore questioned whether proteins actually had specific structures. The direction of research in Bergmann's laboratory was greatly influenced by the arrival of William Howard Stein. At Bergmann's suggestion, Moore and Stein began a long-lived and successful collaboration.
The war interrupted Moore's initial investigation of chromatography--the process of separating the components of a solution--began in the late 1930s. From 1942 to 1945, Moore worked as a technical aide in the National Defense Research Committee of the Office of Scientific Research and Development (OSRD). After the war and following the death of Max Bergmann in 1944, Moore returned to RIMR to resume work with William Howard Stein. This marked a productive period for the two men, leading to their work on chromatographic methods for separating amino acids, peptides (compounds of two or more amino acids), and proteins. Moore's work in chromatography was influenced by the methods of paper chromatography developed by A. J. P. Martin and Richard L. M. Synge of England.
However, limitations in these earlier methods prohibited the study of protein chemistry; new techniques in chromatography had to be developed so that amino acids could be separated. Moore and Stein utilized column chromatography and in 1948 they successfully separated amino acids by passing the solution through a column filled with potato starch. The process was time consuming, however, and presented inadequate separations for amino acid analysis. To facilitate the procedure, Moore and Stein replaced the filler material with a synthetic ion exchange resin, which separated components of a solution by electrical charge and size. In 1949 they successfully separated amino acids from blood and urine.
In 1958 Moore and Stein contributed to the development of the automated amino acid analyzer. The efficiency of the automated technique afforded researchers a tool with which to separate and study the large chemical sequences in protein molecules. This instrument is used worldwide for the study of proteins, enzymes, and hormones as well as the analysis of food.
By 1959 Moore and Stein had determined the amino acid sequence of pancreatic ribonuclease (RNase), a digestive enzyme that breaks down ribonucleic acid (RNA) so that its components can be reused. They discovered that ribonuclease is made up of a chain of 124 amino acids, which they identified and sequenced. This marked the first complete description of the chemical structure of an enzyme, a discovery that earned Moore and Stein the 1972 Nobel Prize in chemistry. They shared the award with Christian Boehmer Anfinsen of the National Institutes of Health.
Understanding protein structure is essential to understanding biological function, which opens the door to the treatment of disease. Moore's findings influenced research in neurochemistry and the study of such diseases as sickle-cell anemia. Scientists later discovered that related ribonucleases are present in nearly all human cells, which prompted studies in the fields of cancer and malaria research. In 1970 Moore and Stein began to investigate deoxyribonuclease, the enzyme that breaks down deoxyribonucleic acid (DNA).
In addition to scientific work, Moore served as editor of The Journal of Biological Chemistry, president of the American Society of Biological Chemistry, received many honors, including membership in the National Academy of Sciences, and was awarded honorary degrees in the United States and Europe.
Moore was diagnosed with amyotrophic lateral sclerosis (Lou Gehrig's disease) in the early 1980s and committed suicide in 1982. Upon his death he left his estate to Rockefeller University.
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This section contains 657 words (approx. 3 pages at 300 words per page) |



