Stanford Moore

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Stanford Moore
Stanford Moore.jpg
Born September 4, 1913
Chicago
DiedAugust 23, 1982 (1982-08-24) (aged 68)
New York City
Nationality U.S.
Alma mater Vanderbilt University
University of Wisconsin–Madison
Known for ribonuclease
Awards Nobel Prize in Chemistry in 1972
Scientific career
Fields biochemistry
Institutions Rockefeller University

Stanford Moore (September 4, 1913 August 23, 1982) was an American biochemist. He shared a Nobel Prize in Chemistry in 1972 (with Christian B. Anfinsen and William Howard Stein, for work done 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.

Biochemist Scientist specialized in biochemistry

Biochemists are scientists that are trained in biochemistry.

Nobel Prize in Chemistry One of the five Nobel Prizes established in 1895 by Alfred Nobel

The Nobel Prize in Chemistry is awarded annually by the Royal Swedish Academy of Sciences to scientists in the various fields of chemistry. It is one of the five Nobel Prizes established by the will of Alfred Nobel in 1895, awarded for outstanding contributions in chemistry, physics, literature, peace, and physiology or medicine. This award is administered by the Nobel Foundation, and awarded by Royal Swedish Academy of Sciences on proposal of the Nobel Committee for Chemistry which consists of five members elected by Academy. The award is presented in Stockholm at an annual ceremony on December 10, the anniversary of Nobel's death.

Christian B. Anfinsen American biochemist

Christian Boehmer Anfinsen Jr. was an American biochemist. He shared the 1972 Nobel Prize in Chemistry with Stanford Moore and William Howard Stein for work on ribonuclease, especially concerning the connection between the amino acid sequence and the biologically active conformation.

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.

Vanderbilt University Private research university in Nashville, Tennessee, United States

Vanderbilt University is a private research university in Nashville, Tennessee. Founded in 1873, it was named in honor of New York shipping and rail magnate Cornelius Vanderbilt, who provided the school its initial $1 million endowment despite having never been to the South. Vanderbilt hoped that his gift and the greater work of the university would help to heal the sectional wounds inflicted by the Civil War.

Phi Kappa Sigma North American collegiate fraternity

Phi Kappa Sigma (ΦΚΣ) is an international all-male college secret and social fraternity. While nicknames differ from institution to institution, the most common nicknames for the fraternity are Skulls, Skullhouse, Phi Kap, and PKS. Phi Kappa Sigma was founded by Dr. Samuel Brown Wylie Mitchell at the University of Pennsylvania. Mitchell recorded the initial ideas and concepts of Phi Kappa Sigma on August 16, 1850. He then began to discuss the idea with other students, first Charles Hare Hutchinson, and then Alfred Victor du Pont, John Thorne Stone, Andrew Adams Ripka, James Bayard Hodge, and Duane Williams. The seven men formally founded the fraternity on October 19, 1850 becoming the founding fathers of Phi Kappa Sigma Phi Kappa Sigma is a charter member of the North-American Interfraternity Conference, and since 2017, is headquartered in Carmel, Indiana. Prior to that, starting with its founding in 1850, the fraternity was based out of Philadelphia, Valley Forge and Chester Springs, Pennsylvania.

University of Wisconsin–Madison Public university in Wisconsin, USA

The University of Wisconsin–Madison is a public research university in Madison, Wisconsin. Founded when Wisconsin achieved statehood in 1848, UW–Madison is the official state university of Wisconsin, and the flagship campus of the University of Wisconsin System. It was the first public university established in Wisconsin and remains the oldest and largest public university in the state. It became a land-grant institution in 1866. The 933-acre (378 ha) main campus, located on the shores of Lake Mendota, includes four National Historic Landmarks. The University also owns and operates a historic 1,200-acre (486 ha) arboretum established in 1932, located 4 miles (6.4 km) south of the main campus.

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. He never married.

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Ribonuclease H enzyme family that degrades the RNA strand of RNA:DNA hybrids

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William Howard Stein was an American biochemist.

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Robert W. Holley American biochemist

Robert William Holley was an American biochemist. He shared the Nobel Prize in Physiology or Medicine in 1968 for describing the structure of alanine transfer RNA, linking DNA and protein synthesis.

Charles Yanofsky was an American geneticist on the faculty of Stanford University who contributed to the establishment of the one gene-one enzyme hypothesis and discovered attenuation, a riboswitch mechanism in which messenger RNA changes shape in response to a small molecule and thus alters its binding ability for the regulatory region of a gene or operon.

The history of molecular biology begins in the 1930s with the convergence of various, previously distinct biological and physical disciplines: biochemistry, genetics, microbiology, virology and physics. With the hope of understanding life at its most fundamental level, numerous physicists and chemists also took an interest in what would become molecular biology.

Bovine pancreatic ribonuclease chemical compound

Bovine pancreatic ribonuclease, also often referred to as bovine pancreatic ribonuclease A or simply RNase A, is a pancreatic ribonuclease enzyme that cleaves single-stranded RNA. Bovine pancreatic ribonuclease is one of the classic model systems of protein science. Two Nobel Prizes in Chemistry have been awarded in recognition of work on bovine pancreatic ribonuclease: in 1972, the Prize was awarded to Christian Anfinsen for his work on protein folding and to Stanford Moore and William Stein for their work on the relationship between the protein's structure and its chemical mechanism; in 1984, the Prize was awarded to Robert Bruce Merrifield for development of chemical synthesis of proteins.

Frederic M. Richards Biochemist, biophysicist, crystallographer, and sailor; founder and chair of Department of Molecular Biophysics and Biochemistry at Yale University

Frederic Middlebrook Richards, commonly referred to as Fred Richards, was an American biochemist and biophysicist known for solving the pioneering crystal structure of the ribonuclease S enzyme in 1967 and for defining the concept of solvent-accessible surface. He contributed many key experimental and theoretical results and developed new methods, garnering over 20,000 journal citations in several quite distinct research areas. In addition to the protein crystallography and biochemistry of ribonuclease S, these included solvent accessibility and internal packing of proteins, the first side-chain rotamer library, high-pressure crystallography, new types of chemical tags such as biotin/avidin, the nuclear magnetic resonance (NMR) chemical shift index, and structural and biophysical characterization of the effects of mutations.

Roger D. Kornberg American chemist

Roger David Kornberg is an American biochemist and professor of structural biology at Stanford University School of Medicine. Kornberg was awarded the Nobel Prize in Chemistry in 2006 for his studies of the process by which genetic information from DNA is copied to RNA, "the molecular basis of eukaryotic transcription."

Anfinsens dogma

Anfinsen's dogma is a postulate in molecular biology that states that, at least for a small globular protein in its standard physiological environment, the native structure is determined only by the protein's amino acid sequence. The dogma was championed by the Nobel Prize Laureate Christian B. Anfinsen from his research on the folding of ribonuclease A. The postulate amounts to saying that, at the environmental conditions at which folding occurs, the native structure is a unique, stable and kinetically accessible minimum of the free energy. The three conditions:

Ribonuclease T<sub>1</sub> chemical compound

Ribonuclease T1 (EC 3.1.27.3, guanyloribonuclease, Aspergillus oryzae ribonuclease, RNase N1, RNase N2, ribonuclease N3, ribonuclease U1, ribonuclease F1, ribonuclease Ch, ribonuclease PP1, ribonuclease SA, RNase F1, ribonuclease C2, binase, RNase Sa, guanyl-specific RNase, RNase G, RNase T1, ribonuclease guaninenucleotido-2'-transferase (cyclizing), ribonuclease N3, ribonuclease N1) is a fungal endonuclease that cleaves single-stranded RNA after guanine residues, i.e., on their 3' end; the most commonly studied form of this enzyme is the version found in the mold Aspergillus oryzae. Owing to its specificity for guanine, RNase T1 is often used to digest denatured RNA prior to sequencing. Similar to other ribonucleases such as barnase and RNase A, ribonuclease T1 has been popular for folding studies.

Pancreatic ribonuclease InterPro Family

Pancreatic ribonucleases are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles.

RNASE1 protein-coding gene in the species Homo sapiens

Ribonuclease pancreatic is an enzyme that in humans is encoded by the RNASE1 gene.

Ralph Franz Hirschmann was a German American chemist who led a team that was responsible for the first organic synthesis of an enzyme, a ribonuclease.

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and structure-function studies on ribonuclease (RNase).

Moses Kunitz (1887-1978) was a Russian-American biochemist who spent most of his career at Rockefeller University. He is best known for a series of experiments in purification and crystallization of proteins, contributing to the determination that enzymes are proteins.

References

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In computing, a Digital Object Identifier orDOI is a persistent identifier or handle used to uniquely identify objects, standardized by the International Organization for Standardization (ISO). An implementation of the Handle System, DOIs are in wide use mainly to identify academic, professional, and government information, such as journal articles, research reports and data sets, and official publications though they also have been used to identify other types of information resources, such as commercial videos.

The Biographical Memoirs of the National Academy of Sciences has been published by the United States National Academy of Sciences since 1877 and presents biographies of selected members. This series of annual volumes, and the analogous British Biographical Memoirs of Fellows of the Royal Society, are "important examples of biographical serials".

National Academy of Sciences science branch of the United States National Academies

The National Academy of Sciences (NAS) is a United States nonprofit, non-governmental organization. NAS is part of the National Academies of Sciences, Engineering, and Medicine, along with the National Academy of Engineering (NAE) and the National Academy of Medicine (NAM).