Stein, William

Stein, William H., (1911-1980), American biochemist and wiimer of the Nobel Prize in Chemistry 1972 (shared with Moore and Anfinsen) for his contribution to the understanding of the cotmection between chemical structure and catalytic activity of the active center of the ribonu-clease molecule. Stein received his Ph.D. in 1938, and in the same year joined the staff of the Rockefeller Institute of Medical... 

Stein, William Howard (1911-80) American biochemist who worked with Stanford Moore to produce a new method of column chromatography by which they were able to separate and identify amino acids from a mix of material produced by the hydrolysis of proteins. Stein, Moore, and Christian Anfmsen shared the 1972 Nobel Prize in chemistry. 

Huber Stein Williams Stein Williams Stein... 

Evans R, Smith I, Munz W D, Williams K J P and Yanwood J 1996 Raman microscopic studies of ceramic coatings based on titanium aluminum nitride ICORS 96 XVth Int. Conf. on Raman Spectroscopy ed S A Asher and P B Stein (New York Wiley) pp 596-7... 

William Howard Stein fl 911-1980) was born in New York City and received his Ph.D. in 1938 from the Columbia College of Physicians and Surgeons. He immediately joined the faculty of the Rockefeller Institute, where he remained until his death. In 1972, he shared the Nobel Prize in chemistry for his work with Stanford Moore on developing methods of amino acid analysis and for determining the structure of ribonuclease. 

Stanford Moore (1913-1982) was born in Chicago, Illinois, and received his Ph.D. from the University of Wisconsin in 1938. He was a professor at the Rockefeller Institute and shared the 1972 Nobel Prize in chemistry with his colleague and collaborator, William Stein. 

To provide some sense of the rate of progress in biochemistry and the rate at which information is generated, Sanger got the primary structure for insuhn, a small protein, in 1955 after several years of dedicated work. We waited 8 years for the next primary structure, that for ribonuclease A, for which a Nobel Prize in Chemistfy (in part) was also awarded, in 1972 to Christian Antinsen, Sanford Moore, and William Stein. There are now tens of thousands of such structures known and the number increases substantially each and every day. The hbrary of known primary structures is collected in several major databases and is accessible to scientists or others who have need of them. ... 

Ashcroft DM, Dimmock P, Garside R, Stein K, Williams HC. Efficacy and tolerability of topical pimecrolimns and tacrolimus in the treatment of atopic dermatitis meta-analysis of randomised controlled trials. BMJ 2005 330 516-21. 

Christian B. Anfinsen, Sanford Moore, and William H. Stein Chemistry Ribonuclease, structure and activity... 

ANFINSEN, CHRISTIAN B. (1916-1995). An American biochemist who won the Nobel prize for chemistry- in 1972 for his work on ribonuclease, especially concerning the connection between the amino acid sequence and die biologically active conformation. He shared the Nobel prize with Stanford Moore and William H. Stein. His doctorate was granted from Harvard. 

M(X)KE. STANFORD (1913-1982). An American biochemist who won the Nobel prize fur chemistry in 1972. with Christian B. Antinscn and William H. Stein, for enzyme studies. He was involved with the analysis ol the action of die complex enzyme deoxyribonuclease. His Ph D. was grunted from the University of Wisconsin. 

Submitted by David Y. Curtin and Allan R. Stein 1 Checked by William G. Dauben and Joel W. Rosenthal... 

Ribonucleases are a widely distributed family of en-zymes that hydrolyze RNA by cutting the P—O ester bond attached to a ribose 5 carbon (fig. 8.12). A good representative of the family is the pancreatic enzyme ribonuclease A (RNase A), which is specific for a pyrimidine base (uracil or cytosine) on the 3 side of the phosphate bond that is cleaved. When the amino acid sequence of bovine RNase A was determined in 1960 by Stanford Moore and William Stein, it was the first enzyme and only the second protein to be sequenced. RNase A thus played an important role in the development of ideas about enzymatic catalysis. It was one of the first enzymes to have its three-dimensional structure elucidated by x-ray diffraction and was also the first to be synthesized completely from its amino acids. The synthetic protein proved to be enzymatically indistinguishable from the native enzyme. 

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