William Eaton (scientist)
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William Eaton (scientist)
William Allen Eaton is a biophysical chemist who is a NIH Distinguished Investigator, Chief of the Section on Biophysical Chemistry, and Chief of the Laboratory of Chemical Physics at the National Institute of Diabetes and Digestive and Kidney Diseases, one of the 20 Institutes of the United States National Institutes of Health. Early life and education Eaton was born and raised in Philadelphia. Like many in his family, he attended the University of Pennsylvania as an undergraduate, majoring in chemistry and graduating in 1959. He then spent one year in Germany as the first Willy Brandt - University of Pennsylvania exchange student at the Free University Berlin. He entered Penn medical school in the Fall of 1960, but discovered that he was more interested in research, particularly after spending the summer of 1962 carrying out research on protein biosynthesis under the supervision of Sydney Brenner at the Laboratory of Molecular Biology, Cambridge, England. He decided to pursue a ...
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Philadelphia, Pennsylvania
Philadelphia, often called Philly, is the largest city in the Commonwealth of Pennsylvania, the sixth-largest city in the U.S., the second-largest city in both the Northeast megalopolis and Mid-Atlantic regions after New York City. Since 1854, the city has been coextensive with Philadelphia County, the most populous county in Pennsylvania and the urban core of the Delaware Valley, the nation's seventh-largest and one of world's largest metropolitan regions, with 6.245 million residents . The city's population at the 2020 census was 1,603,797, and over 56 million people live within of Philadelphia. Philadelphia was founded in 1682 by William Penn, an English Quaker. The city served as capital of the Pennsylvania Colony during the British colonial era and went on to play a historic and vital role as the central meeting place for the nation's founding fathers whose plans and actions in Philadelphia ultimately inspired the American Revolution and the nation's inde ...
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Heme Protein
A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a heme prosthetic group. They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both. The heme consists of iron cation bound at the center of the conjugate base of the porphyrin, as well as other ligands attached to the "axial sites" of the iron. The porphyrin ring is a planar dianionic, tetradentate ligand. The iron is typically Fe2+ or Fe3+. One or two ligands are attached at the axial sites. The porphyrin ring has 4 nitrogen atoms that bind to the iron, leaving two other coordination positions of the iron available for bonding to the histidine of the protein and a divalent atom. Hemeproteins probably evolved to incorporate the iron atom contained within the protoporphyrin IX rin ...
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American Physical Society
The American Physical Society (APS) is a not-for-profit membership organization of professionals in physics and related disciplines, comprising nearly fifty divisions, sections, and other units. Its mission is the advancement and diffusion of knowledge of physics. The society publishes more than a dozen scientific journals, including the prestigious '' Physical Review'' and ''Physical Review Letters'', and organizes more than twenty science meetings each year. APS is a member society of the American Institute of Physics. Since January 2021 the organization has been led by chief executive officer Jonathan Bagger. History The American Physical Society was founded on May 20, 1899, when thirty-six physicists gathered at Columbia University for that purpose. They proclaimed the mission of the new Society to be "to advance and diffuse the knowledge of physics", and in one way or another the APS has been at that task ever since. In the early years, virtually the sole activity of the AP ...
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American Academy Of Arts And Sciences
The American Academy of Arts and Sciences (abbreviation: AAA&S) is one of the oldest learned societies in the United States. It was founded in 1780 during the American Revolution by John Adams, John Hancock, James Bowdoin, Andrew Oliver, and other Founding Fathers of the United States. It is headquartered in Cambridge, Massachusetts. Membership in the academy is achieved through a thorough petition, review, and election process. The academy's quarterly journal, ''Dædalus'', is published by MIT Press on behalf of the academy. The academy also conducts multidisciplinary public policy research. History The Academy was established by the Massachusetts legislature on May 4, 1780, charted in order "to cultivate every art and science which may tend to advance the interest, honor, dignity, and happiness of a free, independent, and virtuous people." The sixty-two incorporating fellows represented varying interests and high standing in the political, professional, and commercial secto ...
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US National Academy Of Sciences
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). As a national academy, new members of the organization are elected annually by current members, based on their distinguished and continuing achievements in original research. Election to the National Academy is one of the highest honors in the scientific field. Members of the National Academy of Sciences serve ''pro bono'' as "advisers to the nation" on science, engineering, and medicine. The group holds a congressional charter under Title 36 of the United States Code. Founded in 1863 as a result of an Act of Congress that was approved by Abraham Lincoln, the NAS is charged with "providing independent, objective advice to the nation on matters related to science and technology. ... to provide scienti ...
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Robert Tycko
Robert Tycko is an American biophysicist whose research primarily involves solid state NMR, including the development of new methods and applications to various areas of physics, chemistry, and biology. He is a member of the Laboratory of Chemical Physics in the National Institute of Diabetes and Digestive and Kidney Diseases at the National Institutes of Health in Bethesda, Maryland, USA. He was formerly a member of the Physical Chemistry Research and Materials Chemistry Research departments of AT&T Bell Labs in Murray Hill, New Jersey. His work has contributed to our understanding of geometric phases in spectroscopy, physical properties of fullerenes, skyrmions in 2D electron systems, protein folding, and amyloid fibrils associated with Alzheimer’s disease and prions. Education Tycko received his bachelor's degree from Princeton University, where he majored in chemistry. He received his Ph.D. in chemistry from the University of California at Berkeley, under the direction of Al ...
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Fellow Of The Royal Society
Fellowship of the Royal Society (FRS, ForMemRS and HonFRS) is an award granted by the judges of the Royal Society of London to individuals who have made a "substantial contribution to the improvement of natural science, natural knowledge, including mathematics, engineering science, and medical science". Fellow, Fellowship of the Society, the oldest known scientific academy in continuous existence, is a significant honour. It has been awarded to many eminent scientists throughout history, including Isaac Newton (1672), Michael Faraday (1824), Charles Darwin (1839), Ernest Rutherford (1903), Srinivasa Ramanujan (1918), Albert Einstein (1921), Paul Dirac (1930), Winston Churchill (1941), Subrahmanyan Chandrasekhar (1944), Dorothy Hodgkin (1947), Alan Turing (1951), Lise Meitner (1955) and Francis Crick (1959). More recently, fellowship has been awarded to Stephen Hawking (1974), David Attenborough (1983), Tim Hunt (1991), Elizabeth Blackburn (1992), Tim Berners-Lee (2001), Venki R ...
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Marius Clore
G. Marius Clore MAE, FRSC, FRS is a British-born, Anglo-American molecular biophysicist and structural biologist. He was born in London, U.K. and is a dual US/U.K. Citizen. He is a Member of the National Academy of Sciences, a Fellow of the Royal Society, a NIH Distinguished Investigator, and the Chief of the Molecular and Structural Biophysics Section in the Laboratory of Chemical Physics of the National Institute of Diabetes and Digestive and Kidney Diseases at the U.S. National Institutes of Health. He is known for his foundational work in three-dimensional protein and nucleic acid structure determination by biomolecular NMR spectroscopy, for advancing experimental approaches to the study of large macromolecules and their complexes by NMR, and for developing NMR-based methods to study rare conformational states in protein- nucleic acid and protein-protein recognition. Clore's discovery of previously undetectable, functionally significant, rare transient states of macro ...
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Ad Bax
Adriaan "Ad" Bax (born 1956) is a Dutch-American molecular biophysicist. He was born in the Netherlands and is the Chief of the Section on Biophysical NMR Spectroscopy at the National Institutes of Health. He is known for his work on the methodology of biomolecular NMR spectroscopy. Biography Bax was born in the Netherlands. He studied at Delft University of Technology where he got his engineer's degree (Ir. degree) in 1978, and Ph.D. degree in applied physics in 1981, after spending considerable time working with Ray Freeman at Oxford University. He worked as a postdoc with Gary Maciel at Colorado State University, before joining the NIH's Laboratory of Chemical Physics in 1983. In 1994 he became correspondent of the Royal Netherlands Academy of Arts and Sciences. He is currently the Chief of the Section on Biophysical NMR Spectroscopy at NIH. In 2002 he was elected a member of the National Academy of Sciences in the section on Biophysics and computational biology and a Fellow o ...
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Protein Folding
Protein folding is the physical process by which a protein chain is translated to its native three-dimensional structure, typically a "folded" conformation by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA to a linear chain of amino acids. At this stage the polypeptide lacks any stable (long-lasting) three-dimensional structure (the left hand side of the first figure). As the polypeptide chain is being synthesized by a ribosome, the linear chain begins to fold into its three-dimensional structure. Folding of many proteins begins even during translation of the polypeptide chain. Amino acids interact with each other to produce a well-defined three-dimensional structure, the folded protein (the right hand side of the figure), ...
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Sickle-cell Anemia
Sickle cell disease (SCD) is a group of blood disorders typically inherited from a person's parents. The most common type is known as sickle cell anaemia. It results in an abnormality in the oxygen-carrying protein haemoglobin found in red blood cells. This leads to a rigid, sickle-like shape under certain circumstances. Problems in sickle cell disease typically begin around 5 to 6 months of age. A number of health problems may develop, such as attacks of pain (known as a sickle cell crisis), anemia, swelling in the hands and feet, bacterial infections and stroke. Long-term pain may develop as people get older. The average life expectancy in the developed world is 40 to 60 years. Sickle cell disease occurs when a person inherits two abnormal copies of the β-globin gene (''HBB'') that makes haemoglobin, one from each parent. This gene occurs in chromosome 11. Several subtypes exist, depending on the exact mutation in each haemoglobin gene. An attack can be set off by temp ...
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Hemoglobin
Hemoglobin (haemoglobin BrE) (from the Greek word αἷμα, ''haîma'' 'blood' + Latin ''globus'' 'ball, sphere' + ''-in'') (), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein present in red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae) as well as the tissues of some invertebrates. Hemoglobin in blood carries oxygen from the respiratory organs (''e.g.'' lungs or gills) to the rest of the body (''i.e.'' tissues). There it releases the oxygen to permit aerobic respiration to provide energy to power functions of an organism in the process called metabolism. A healthy individual human has 12to 20grams of hemoglobin in every 100mL of blood. In mammals, the chromoprotein makes up about 96% of the red blood cells' dry content (by weight), and around 35% of the total content (including water). Hemoglobin has an oxygen-binding capacity of 1.34mL O2 per gram, which increases the total blood oxygen ...
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