Daniel E. Koshland Jr. | |
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Koshland in 1991
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Born |
New York City |
March 30, 1920
Died | July 23, 2007 Lafayette, California |
(aged 87)
Fields | Biochemistry |
Institutions | University of California at Berkeley |
Alma mater |
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Known for | Induced fit model |
Notable awards | |
Spouse |
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Children |
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Daniel Edward Koshland Jr. (March 30, 1920 – July 23, 2007) was an American biochemist. He reorganized the study of biology at the University of California, Berkeley, and was the editor of the leading US science journal, Science, from 1985 to 1995. He was a Member of the United States National Academy of Sciences.
Koshland is one of three children born to a Jewish family, the son of Daniel E. Koshland Sr. and Eleanor Haas, daughter of the Haas family patriarch Abraham Haas. He has two siblings: Frances "Sissy" Koshland Geballe and Phyllis Koshland Friedman. His father served as CEO of Levi Strauss & Co. from 1955 to 1958 and is widely credited with saving the company during the Great Depression.
Koshland's private fortune, derived from Levi Strauss, put him on lists of America's wealthiest people. Rather than relying on his fortune, Koshland chose to pursue a career in science. Koshland wrote in an autobiographical article that he decided to become a scientist in the eighth grade after reading two popular books about science, Microbe Hunters by Paul de Kruif and Arrowsmith by Sinclair Lewis.
Attending Phillips Exeter Academy for high school Koshland then became the third generation of his family to matriculate to the University of California at Berkeley (UCB) where he majored in chemistry. The next five years, 1941–46, were spent working with Glenn T. Seaborg at the University of Chicago on the top-secret Manhattan project, where his team purified the plutonium that was used to make the atomic bomb at Los Alamos.
In 1949, he received his Ph.D. in organic chemistry from the University of Chicago. His early work was in enzyme kinetics at Brookhaven National Laboratory, Long Island, and Rockefeller University, New York. This led him to propose the induced fit model for enzyme catalysis. After this advance, he turned to studying how bacteria control their movements in chemotaxis. Dr. Koshland's laboratory made three major discoveries concerning protein phosphorylation in bacteria. (1) The first phosphorylated bacterial protein, isocitrate dehydrogenase, was identified. (2) It was demonstrated that substituting an aspartate residue for the serine residue that was phosphorylated causes the protein to behave as if it were phosphorylated. (3) The response regulators in the two-component regulatory systems were shown to be phosphorylated on an aspartate residue and to be protein phosphatases with a covalent intermediate.