1.
Enzyme
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Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions, the molecules at the beginning of the process upon which enzymes may act are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life, the set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology, enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules, enzymes specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy, some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5-phosphate decarboxylase, which allows a reaction that would take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules, inhibitors are molecules that decrease enzyme activity, many drugs and poisons are enzyme inhibitors. An enzymes activity decreases markedly outside its optimal temperature and pH, some enzymes are used commercially, for example, in the synthesis of antibiotics. French chemist Anselme Payen was the first to discover an enzyme, diastase and he wrote that alcoholic fermentation is an act correlated with the life and organization of the yeast cells, not with the death or putrefaction of the cells. In 1877, German physiologist Wilhelm Kühne first used the term enzyme, the word enzyme was used later to refer to nonliving substances such as pepsin, and the word ferment was used to refer to chemical activity produced by living organisms. Eduard Buchner submitted his first paper on the study of yeast extracts in 1897, in a series of experiments at the University of Berlin, he found that sugar was fermented by yeast extracts even when there were no living yeast cells in the mixture. He named the enzyme that brought about the fermentation of sucrose zymase, in 1907, he received the Nobel Prize in Chemistry for his discovery of cell-free fermentation. Following Buchners example, enzymes are usually named according to the reaction they carry out, the biochemical identity of enzymes was still unknown in the early 1900s. Sumner showed that the enzyme urease was a protein and crystallized it. These three scientists were awarded the 1946 Nobel Prize in Chemistry, the discovery that enzymes could be crystallized eventually allowed their structures to be solved by x-ray crystallography. This high-resolution structure of lysozyme marked the beginning of the field of structural biology, an enzymes name is often derived from its substrate or the chemical reaction it catalyzes, with the word ending in -ase
2.
Anaerobic bacteria
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An anaerobic organism or anaerobe is any organism that does not require oxygen for growth. It may react negatively or even die if oxygen is present, an anaerobic organism may be unicellular or multicellular. Van Leeuwenhoek sealed one of the tubes by using a flame. In 1913 Martinus Beijerinck repeated Van Leeuwenhoeks experiment and identified Clostridium butyricum as a prominent anaerobic bacterium in the sealed pepper infusion tube liquid. That Leeuwenhoek, one hundred years before the discovery of oxygen, for practical purposes, there are three categories of anaerobe, Obligate anaerobes, which are harmed by the presence of oxygen. Aerotolerant organisms, which use oxygen for growth, but tolerate its presence. Facultative anaerobes, which can grow without oxygen but use oxygen if it is present, some obligate anaerobes use fermentation, while others use anaerobic respiration. In the presence of oxygen, facultative anaerobes use aerobic respiration, without oxygen, some of them ferment, there are many anaerobic fermentative reactions. This is only 5% of the energy per molecule that the typical aerobic reaction generates. Since normal microbial culturing occurs in air, which is an aerobic environment. Hydrogen then reacts with oxygen gas on a palladium catalyst to more water. The issue with the Gaspak method is that a reaction can take place where the bacteria may die. The thioglycollate supplies a medium mimicking that of a dicot, thus providing not only an anaerobic environment, complex multicellular life that does not need oxygen is said to be rare, however there are examples of such organisms. Some organisms metabolise primarily using glycogen, for example the Nereid s and some polychaetes, or the juvenile Trichinella spiralis parasites. )
3.
National Medal of Science
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The twelve member presidential Committee on the National Medal of Science is responsible for selecting award recipients and is administered by the National Science Foundation. The National Medal of Science was established on August 25,1959, the medal was originally to honor scientists in the fields of the physical, biological, mathematical, or engineering sciences. The Committee on the National Medal of Science was established on August 23,1961, on January 7,1979, the American Association for the Advancement of Science passed a resolution proposing that the medal be expanded to include the social and behavioral sciences. In response, Senator Ted Kennedy introduced the Science and Technology Equal Opportunities Act into the Senate on March 7,1979, President Jimmy Carters signature enacted this change as Public Law 96-516 on December 12,1980. The first National Medal of Science was awarded on February 18,1963, the first woman to receive a National Medal of Science was Barbara McClintock, who was awarded for her work on plant genetics in 1970. Although Public Law 86-209 provides for 20 recipients of the medal per year, it is typical for approximately 8–15 accomplished scientists, there have been a number of years where no National Medals of Science were awarded. Those years include,1985,1984,1980,1978,1977,1972 and 1971, the awards ceremony is organized by the Office of Science and Technology Policy. It takes place at the White House and is presided by the sitting United States president, each year the National Science Foundation sends out a call to the scientific community for the nomination of new candidates for the National Medal of Science. Individuals are nominated by their peers with each nomination requiring three letters of support from individuals in science and technology, the nomination of a candidate is effective for three years, at the end of three years, the candidates peers are allowed to renominate the candidate. The Committee makes their recommendations to the President for the final awarding decision, the National Medal of Science depicts Man, surrounded by earth, sea, and sky, contemplating and struggling to understand Nature. The crystal in his hand represents the order and also suggests the basic unit of living things. The formula being outlined in the sand symbolizes scientific abstraction
4.
Jimmy Carter
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James Earl Jimmy Carter Jr. is an American politician who served as the 39th President of the United States from 1977 to 1981. In 2002, he was awarded the Nobel Peace Prize for his work with the Carter Center, Carter was a Democrat who was raised in rural Georgia. He was a farmer who served two terms as a Georgia State Senator from 1963 to 1967, and one as the Governor of Georgia from 1971 to 1975. He was elected President in 1976, defeating incumbent President Gerald Ford in a close election. On his second day in office, Carter pardoned all evaders of the Vietnam War drafts, during Carters term as President, two new cabinet-level departments, the Department of Energy and the Department of Education, were established. He established an energy policy that included conservation, price control. In foreign affairs, Carter pursued the Camp David Accords, the Panama Canal Treaties, the round of Strategic Arms Limitation Talks. On the economic front he confronted persistent stagflation, a combination of inflation, high unemployment. The end of his tenure was marked by the 1979–1981 Iran hostage crisis, the 1979 energy crisis, the Three Mile Island nuclear accident. In response to the Soviet move he ended détente, escalated the Cold War, Carter won the 1980 primary with 51. 13% of the vote but lost the general election in an electoral landslide to Republican nominee Ronald Reagan, who won 44 of 50 states. His presidency has drawn medium-low responses from historians, with many considering him to have accomplished more with his post-presidency work and he set up the Carter Center in 1982 as his base for advancing human rights. He has also traveled extensively to conduct negotiations, observe elections. Additionally, Carter is a key figure in the Habitat for Humanity project, since surpassing Herbert Hoover in September 2012, he has been the longest-retired president in American history. He is also the first president to mark the 40th anniversary of his election and inauguration, in reference to current political views, he has criticized some of Israels actions and policies in regards to the Israeli–Palestinian conflict and has advocated for a two-state solution. James Earl Carter, Jr. was born on October 1,1924, at the Wise Sanitarium in Plains and he is a descendant of English immigrant Thomas Carter, who settled in Virginia in 1635. Numerous generations of Carters lived as farmers in Georgia. Carter is also a descendant of Thomas Cornell, an ancestor of Cornell Universitys founder and of Richard Nixon, Plains was a boomtown of 600 people at the time of Carters birth. His father, James Earl Carter, Sr. was a local businessman who ran a general store and had begun to invest in farmland
5.
National Heart Institute
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The National Heart, Lung, and Blood Institute is the third largest Institute of the National Institutes of Health, located in Bethesda, Maryland, United States. It is tasked with allocating about $3, nHLBIs Director is Gary H. Gibbons. Research is related to the causes, prevention, diagnosis, and treatment of heart, blood vessel, lung, and blood diseases and it also supports research on clinical use of blood and all aspects of the management of blood resources. For health professionals and the public, the NHLBI conducts educational activities, including development and dissemination of materials in the above areas, the NHLBI coordinates relevant activities in the above areas, including the related causes of stroke, with other research institutes and federal health programs. There are 60 investigators, each of whom runs their own research program and they are supported by a group of core services that implement state-of-the-art techniques available to all NHLBI investigators. The NHLBI was home to Marshall Nirenberg, Nobel laureate for his part in the discovery of the genetic code, the DIR also has a large training component, with opportunities for undergraduate, graduate, and medical students as well as post-doctoral training. The NHLBI sponsors National Wear Red Day and the Heart Truth campaign, a national awareness campaign for women about heart disease
6.
National Academy of Sciences
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The National Academy of Sciences 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, 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 Academies is one of the highest honors in the scientific field, members 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, … to provide scientific advice to the government whenever called upon by any government department. The Academy receives no compensation from the government for its services, as of 2016, the National Academy of Sciences includes about 2,350 members and 450 foreign associates. It employed about 1,100 staff in 2005, the current members annually elect new members for life. Approximately 200 members have won a Nobel Prize, the National Academy of Sciences is a member of the International Council for Science. Although there is no relationship with state and local academies of science. The National Academies is governed by a 17-member Council, made up of five officers and 12 Councilors, the National Academy of Sciences meets annually in Washington, D. C. which is documented in the Proceedings of the National Academy of Sciences, its scholarly journal. The National Academies Press is the publisher for the National Academies, since 2004, the National Academy of Sciences has administered the Marian Koshland Science Museum to provide public exhibits and programming related to its policy work. The museums current exhibits focus on change and infectious disease. The National Academy of Sciences maintains multiple buildings around the United States, the building has a neoclassical architectural style and was built by architect Bertram Grosvenor Goodhue. The building was dedicated in 1924 and is listed on the National Register of Historic Places, the building is used for lectures, symposia, exhibitions, and concerts, in addition to annual meetings of the NAS, NAE, and NAM. The 2012 Presidential Award for Math and Science Teaching ceremony was held here on March 5,2014, approximately 150 staff members work at the NAS Building. More than 1,000 National Academies staff members work at The Keck Center of the National Academies at 500 Fifth Street in northwest Washington, the Keck Center provides meeting space and houses the National Academies Press Bookstore. The NAS also maintains conference centers in California and Massachusetts, the J. Erik Jonsson Conference Center located at 314 Quissett Avenue in Woods Hole, Massachusetts, is another conference facility. The Act of Incorporation, signed by President Abraham Lincoln on March 3,1863, created the National Academy of Sciences, many of the original NAS members came from the so-called Scientific Lazzaroni, an informal network of mostly physical scientists working in the vicinity of Cambridge, Massachusetts. Senator Henry Wilson of Massachusetts was to name Agassiz to the Board of Regents of the Smithsonian Institution, Agassiz was to come to Washington at the governments expense to plan the organization with the others
7.
The Washington Post
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The Washington Post is an American daily newspaper. It is the most widely circulated newspaper published in Washington, D. C. and was founded on December 6,1877 and its current slogan is Democracy Dies in Darkness. Located in the city of the United States, the newspaper has a particular emphasis on national politics. Daily editions are printed for the District of Columbia, Maryland, the newspaper is published as a broadsheet, with photographs printed both in color and in black and white. The newspaper has won 47 Pulitzer Prizes and this includes six separate Pulitzers awarded in 2008, the second-highest number ever awarded to a single newspaper in one year, second only to The New York Times seven awards in 2002. Post journalists have also received 18 Nieman Fellowships and 368 White House News Photographers Association awards, in years since, its investigations have led to increased review of the Walter Reed Army Medical Center. In 2013, its owners, the Graham family, sold the newspaper to billionaire entrepreneur. The newspaper is owned by Nash Holdings LLC, a holding company Bezos created for the acquisition, the Washington Post is generally regarded as one of the leading daily American newspapers, along with The New York Times and The Wall Street Journal. The Post has distinguished itself through its reporting on the workings of the White House, Congress. It is one of the two daily broadsheets published in Washington D. C. the other being its smaller rival The Washington Times, unlike The New York Times and The Wall Street Journal, The Washington Post does not print an edition for distribution away from the East Coast. In 2009, the newspaper ceased publication of its National Weekly Edition, the majority of its newsprint readership is in District of Columbia and its suburbs in Maryland and Northern Virginia. The Sunday Style section differs slightly from the weekday Style section, it is in a tabloid format, and it houses the reader-written humor contest The Style Invitational. Additional weekly sections appear on weekdays, Health & Science on Tuesday, Food on Wednesday, Local Living on Thursday, the latter two are in a tabloid format. In November 2009, it announced the closure of its U. S. regional bureaus—Chicago, Los Angeles and New York—as part of a focus on. political stories. The newspaper has bureaus in Maryland and Virginia. While its circulation has been slipping, it has one of the highest market-penetration rates of any metropolitan news daily, for many decades, the Post had its main office at 1150 15th Street NW. This real estate remained with Graham Holdings when the newspaper was sold to Jeff Bezos Nash Holdings in 2013, Graham Holdings sold 1150 15th Street for US$159 million in November 2013. The Washington Post continued to lease space at 1150 L Street NW, in May 2014, The Washington Post leased the west tower of One Franklin Square, a high-rise building at 1301 K Street NW in Washington, D. C
8.
Thressa Stadtman
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Thressa Campbell Stadtman was an American biochemist, notable for her discovery of selenocysteine, and her research on selenoproteins and bioenergetics. In addition she made significant advances in amino acid metabolism, enzymes dependent on vitamin B12, in 1920, she was born in Sterling, New York. In 1940, she graduated from Cornell University, with a B. S. in Microbiology, in 1949, she graduated from University of California, Berkeley, with a Ph. D. in Microbial Biochemistry. Her thesis was titled Studies on Methane Fermentations and she was the wife of Earl Reece Stadtman whom she met when they were both graduate students at the University of California, Berkeley. The both were hired by what was then the National Heart Institute in 1950 becoming the first husband-and-wife team at the National Institutes of Health and they both oversaw their own biochemistry labs and collaborated closely. In 2005, they were honored by the NIH with an exhibit titled The Stadtman Way, A Tale of Two Biochemists at NIH. Over a 60-year period, starting in 1943, she published 212, Stadtman was elected a member of the National Academy of Sciences in 1981. Stadtman died in December 2016 at the age of 96, Stadtman by Buhm Soon Park, January 2001
9.
Selenocysteine
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Selenocysteine is the 21st proteinogenic amino acid. Selenocysteine exists naturally in three domains of life, but not in lineage, as a building block of selenoproteins. Selenocysteine is an analogue with a selenium-containing selenol group in place of the sulfur-containing thiol group. Selenocysteine is present in several enzymes, Selenocysteine was discovered by biochemist Thressa Stadtman at the National Institutes of Health. Selenocysteine has a similar to that of cysteine, but with an atom of selenium taking the place of the usual sulfur. Proteins that contain one or more residues are called selenoproteins. Most selenoproteins contain a single Sec residue, selenoproteins with catalytic activities which depend on selenocysteines biochemical activity are called selenoenzymes. The structurally characterized selenoenzymes have been found to employ catalytic triad structures that influence the nucleophilicity of the active site selenocysteine, Selenocysteine has both a lower pKa and a lower reduction potential than cysteine. These properties make it suitable in proteins that are involved in antioxidant activity. Although it is found in the three domains of life, it is not universal in all organisms, unlike other amino acids present in biological proteins, selenocysteine is not coded for directly in the genetic code. Instead, it is encoded in a way by a UGA codon. Such a mechanism is called translational recoding and its efficiency depends on the selenoprotein being synthesized, when cells are grown in the absence of selenium, translation of selenoproteins terminates at the UGA codon, resulting in a truncated, nonfunctional enzyme. The UGA codon is made to encode selenocysteine by the presence of an insertion sequence in the mRNA. The SECIS element is defined by nucleotide sequences and secondary structure base-pairing patterns. In bacteria, the SECIS element is located immediately following the UGA codon within the reading frame for the selenoprotein. In Archaea and in eukaryotes, the SECIS element is in the 3 untranslated region of the mRNA, again unlike the other amino acids, no free pool of selenocysteine exists in the cell. Its high reactivity would cause damage to cells, instead, cells store selenium in the less reactive selenide form. Selenocysteine synthesis occurs on a specialized tRNA, which functions to incorporate it into nascent polypeptides
10.
Carrizozo, New Mexico
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Carrizozo is a town in Lincoln County, New Mexico and is the county seat with a population of 996 at the 2010 census. Founded in 1899, the town provided the railroad access for Lincoln County. However, with declining relevance of the railroad, the population of the town has gradually declined, the town is located at the intersection of U. S. Route 54 and U. S. Route 380. The name of the town is derived from the Spanish vernacular for reed grass, the additional zo at the end of the town name was added to indicate abundance of Carrizo grass. The town is now referred to as Zozo. Prior to 1899, the area was primarily a few ranches, lawrence Murphy, a merchant active in the Lincoln County War, owned a major ranch in the area. The location of Carrizozo was selected as the site for a station on the El Paso, Carrizozo was chosen over the nearby booming mine town of White Oaks, New Mexico, resulting in large-scale migration from White Oaks to Carrizozo. The railroad brought businesses, growing populations, and increased importance to the town of Carrizozo, as a result, a county referendum in 1909 moved the county seat of Lincoln County from the town of Lincoln to Carrizozo. This decision resulted in a legal battle that was eventually resolved in favor of Carrizozo by the United States Supreme Court in the case of Gray v. Taylor. The result was a period where railroad access and political importance combined to lead to significant population growth in Carrizozo. The population reached around 2,000 by 1920, during the same time, journalist Quentin Reynolds visited the town and wrote a piece on it for Colliers Weekly. Later, he wrote in The Wounded Dont Cry that I used to agree with Bugs that once you left New York, you were strictly on the horse, but of late years I’ve had to modify that. Since then I’ve discovered New Orleans, San Francisco and a place called Carrizozo, New Mexico. I want to go there and gang around the drug store, Carrizozo is about 50 miles from Trinity Site, where the first nuclear bomb was detonated on July 16,1945. Residents reported tremors like an earthquake and, as the first major downwind settlement, with the rise of the automobile, Carrizozos proximity to the railroad became less important starting in the 1950s, and the last passenger train passed through in 1968. The result was a decrease in economic opportunity in Carrizozo, recently, the town has seen increasing focus on tourism, and cherry cider produced in the town is known nationally. Carrizozo is located at the point of the Tularosa Basin which extends southward to the New Mexico-Texas border. The town itself is located in an area known prior to the founding of the town as the Corrizo flats
11.
University of California, Berkeley
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The University of California, Berkeley, is a public research university located in Berkeley, California. In 1960s, UC Berkeley was particularly noted for the Free Speech Movement as well as the Anti-Vietnam War Movement led by its students. S, Department of Energy, and is home to many world-renowned research institutes and organizations including Mathematical Sciences Research Institute and Space Sciences Laboratory. Faculty member J. R. Oppenheimer, the father of the atomic bomb, Lawrence Livermore Lab also discovered or co-discovered six chemical elements. The Academic Ranking of World Universities also ranks the University of California, Berkeley, third in the world overall, in 1866, the private College of California purchased the land comprising the current Berkeley campus. Ten faculty members and almost 40 students made up the new University of California when it opened in Oakland in 1869, billings was a trustee of the College of California and suggested that the college be named in honor of the Anglo-Irish philosopher George Berkeley. In 1870, Henry Durant, the founder of the College of California, with the completion of North and South Halls in 1873, the university relocated to its Berkeley location with 167 male and 22 female students and held its first classes. In 1905, the University Farm was established near Sacramento, ultimately becoming the University of California, by the 1920s, the number of campus buildings had grown substantially, and included twenty structures designed by architect John Galen Howard. Robert Gordon Sproul served as president from 1930 to 1958, by 1942, the American Council on Education ranked UC Berkeley second only to Harvard University in the number of distinguished departments. During World War II, following Glenn Seaborgs then-secret discovery of plutonium, UC Berkeley physics professor J. Robert Oppenheimer was named scientific head of the Manhattan Project in 1942. Along with the Lawrence Berkeley National Laboratory, Berkeley is now a partner in managing two other labs, Los Alamos National Laboratory and Lawrence Livermore National Laboratory, originally, military training was compulsory for male undergraduates, and Berkeley housed an armory for that purpose. In 1917, Berkeleys ROTC program was established, and its School of Military Aeronautics trained future pilots, including Jimmy Doolittle, both Robert McNamara and Frederick C. Weyand graduated from UC Berkeleys ROTC program, earning B. A. degrees in 1937 and 1938, in 1926, future fleet admiral Chester W. Nimitz established the first Naval Reserve Officers Training Corps unit at Berkeley. The Board of Regents ended compulsory military training at Berkeley in 1962, during the McCarthy era in 1949, the Board of Regents adopted an anti-communist loyalty oath. A number of faculty members objected and were dismissed, ten years passed before they were reinstated with back pay, in 1952, the University of California became an entity separate from the Berkeley campus. Each campus was given autonomy and its own Chancellor. Then-president Sproul assumed presidency of the entire University of California system, Berkeley gained a reputation for student activism in the 1960s with the Free Speech Movement of 1964 and opposition to the Vietnam War. In the highly publicized Peoples Park protest in 1969, students and the school conflicted over use of a plot of land, then governor of California Ronald Reagan called the Berkeley campus a haven for communist sympathizers, protesters, and sex deviants. Modern students at Berkeley are less active, with a greater percentage of moderates and conservatives
12.
David E. Green
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David Ezra Green was an American biochemist who made significant contributions to the study of enzymes, particularly the electron transport chain and oxidative phosphorylation. Green was born in Brooklyn, New York, the son of Jennie and Hyman Levy Green and his parents were Jewish immigrants from Russia and Germany. He was awarded a degree in biology from New York University and he then moved to England and worked for eight years at the University of Cambridge under the supervision of Malcolm Dixon, on redox reactions in biological systems. He received his PhD under Dixon in 1934 with a thesis entitled The Application of Oxidation-Reduction Potentials to Biological Systems, at the outbreak of the Second World War, Green moved back to America and established himself in a laboratory at Columbia University. Here he studied the metabolism of amino acids and the citric acid cycle and he was married to English-born Doris Cribb. He is the father of biochemist Rowena Green Matthews and grandfather of Wisconsin Senator Tammy Baldwin, national Academy of Sciences Biographical Memoir
13.
Britton Chance
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At the 1952 Summer Olympics, Chance won a gold medal in sailing. Chance was born in Wilkes-Barre, Pennsylvania and he received a B. A. M. A. and Ph. D. degree in Physical Chemistry at the University of Pennsylvania, where he was a member of St. Anthony Hall. Chance earned a second Ph. D. at Cambridge University in 1942 in Biology/Physiology, during World War II, Chance worked for the Radiation Laboratory at the Massachusetts Institute of Technology which was working on the development of radar. In 1952, he received his D. Sc. from Cambridge and he was promoted as the Professor of Biophysics at the University of Pennsylvania School of Medicine and appointed the second director of the Johnson Foundation, a position he held until 1983. He was then appointed E. R. Johnson Professor of Biophysics and Physical Biochemistry in 1964, in his early career, he was mainly working on enzyme structure and function. He had invented the now standard stopped-flow device to measure the existence of the complex in enzyme reaction. He was a pioneer in the simulations of biochemical reactions. He won a medal for the United States at the 1952 Summer Olympics in the 5½ Meter Class, alongside Edgar White. Chance joined the United States National Academy of Sciences in 1952 and he received the National Medal of Science in 1974. He was also elected a Foreign Member of the Royal Swedish Academy of Sciences, Medical Sciences, in 1968. He died in the Hospital of the University of Pennsylvania, Philadelphia in November 2010, mDs from, Karolinska Institute, University of Düsseldorf, University of Buenos Aires, University of Copenhagen, Universita Degli Studi Di Roma Tor Vergata. D. Sc. degrees from, Medical College of Ohio at Toledo in 1974, Semmelweis University in 1976, Hahnemann Medical College in 1977, University of Pennsylvania in 1985 and he was also made an Overseas Fellow of Churchill College, Cambridge. Paul-Lewis Award in Enzyme Chemistry, in 1950 John Price Wetherill Medal, in 1966 Gold Medal for Distinguished Service to Medicine, College of Physicians, USA, Gold Medal, Society of Magnetic Resonance in Medicine, USA, in 1988. This award was first presented in 2004 during the conference of ISOTT in Bari. SPIE has established Britton Chance Biomedical Optics Award, honoring his significant contribution to biomedical optics, the award will be presented annually to recognize outstanding contributions to the field of biomedical optics through the development of innovative, high-impact biophotonic technologies. Britton Chance Britton Chance, His Life, Times, And Legacy 100 Greatest Discoveries - Biology Britton Chance Papers, American Philosophical Society
14.
Arthur Kornberg
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He was also awarded the Paul-Lewis Award in Enzyme Chemistry from the American Chemical Society in 1951, L. H. D. degree from Yeshiva University in 1962, as well as National Medal of Science in 1979. Born in New York City, Arthur Kornberg was the son of Jewish parents Joseph and Lena Kornberg and his paternal grandfather had changed the family name from Queller to avoid the draft by taking on the identity of someone who had already completed military service. Joseph spoke at least six languages although he had no formal education, Arthur Kornberg was educated first at Abraham Lincoln High School and then at City College in New York City. He received at B. Sc. in 1937, followed by an M. D. at the University of Rochester in 1941, the results were published in Kornbergs first research paper in 1942. Kornbergs internship was at Strong Memorial Hospital in Rochester, New York, after completing his medical training, he joined the armed services as a Lieutenant in the United States Coast Guard, serving as a ships doctor in 1942. Rolla Dyer, the Director of National Institutes of Health, had noticed his paper, from 1942 to 1945, Kornbergs work was the feeding of specialized diets to rats to discover new vitamins. The feeding of rats was boring work, and Kornberg became fascinated by enzymes and he became Chief of the Enzyme and Metabolism Section at NIH from 1947–1953, working on understanding of ATP production from NAD and NADP. This led to his work on how DNA is built up from simpler molecules, in 1953 he became Professor and Head of the Department of Microbiology, Washington University in St. Louis, until 1959. Here he continued experimenting with the enzymes which created DNA, in 1956 he isolated the first DNA polymerizing enzyme, now known as DNA polymerase I. This won him the Nobel prize in 1959, in 1960 he received a LL. D. Again from City College, followed by a D. Sc. at the University of Rochester in 1962, Kornbergs mother died of gas gangrene from a spore infection after a routine gall bladder operation in 1939. This started his fascination with spores, and he devoted some of his research efforts to understanding them while at Washington University. This was an unfashionable but complex area of science, and although some progress was made, the Arthur Kornberg Medical Research Building at the University of Rochester Medical Center was named in his honor in 1999. Until his death, Kornberg maintained a research laboratory at Stanford. For several years the focus of his research was the metabolism of inorganic polyphosphate, richardson, Randy Schekman, William T. Wickner, James Rothman, Arturo Falaschi and Ken-ichi Arai. On November 21,1943, Kornberg married Sylvy Ruth Levy and she worked closely with Kornberg and contributed significantly to the discovery of DNA polymerase. The day after he was awarded the Nobel prize, she was quoted in a newspaper as saying I was robbed, Arthur and Sylvy Kornberg had three sons, Roger David Kornberg, Thomas B. Roger is Professor of Structural Biology at Stanford University, and the 2006 laureate of the Nobel Prize in Chemistry, Thomas discovered DNA polymerase II and III in 1970 and is now a professor at the University of California, San Francisco
15.
Paul D. Boyer
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Paul Delos Boyer is an American biochemist, analytical chemist, and a professor of chemistry at University of California Los Angeles. He is the oldest living Nobel laureate at age 98, Boyer was born in Provo, Utah. He grew up in a nonpracticing Mormon family and he attended Provo High School, where he was active in student government and the debating team. He received a B. S. in chemistry from Brigham Young University in 1939, five days before leaving for Wisconsin, Paul married Lyda Whicker. They remain married and have three children, Gail B, Hayes, Alexandra Boyer and Dr. Douglas Boyer, and eight grandchildren, Imran Clark, Mashuri Clark, Rashid Clark, Djahari Clark, Faisal Clark, Lisa A. Hayes, Leah Boyer and Josh Boyer. After experimenting with Unitarianism, Boyer eventually became an atheist, in 2003 he was one of 22 Nobel Laureates who signed the Humanist Manifesto. He began his independent research career at the University of Minnesota and introduced kinetic, isotopic, in 1955, he received a Guggenheim Fellowship and worked with Professor Hugo Theorell on the mechanism of alcohol dehydrogenase. In 1956, he accepted a Hill Foundation Professorship and moved to the campus of the University of Minnesota. In 1959-1960, he served as Chairman of the Biochemistry Section of the American Chemical Society, since 1963, he has been a Professor in the Department of Chemistry and Biochemistry at University of California, Los Angeles. In 1965, he became the Founding Director of the Molecular Biology Institute and spearheaded the construction of the building, Paul Boyer was Editor or Associate Editor of the Annual Review of Biochemistry from 1963-1989. He was Editor of the series, The Enzymes. In 1981, he was Faculty Research Lecturer at UCLA, in that same year, he was awarded the prestigious Tolman Medal by the Southern California Section of the American Chemical Society. Dahms, A. S. & P. D. Boyer, kanazawa, T. & P. D. Boyer. Occurrence and Characteristics of a Rapid Exchange of Phosphate Oxygens Catalyzed by Sarcoplasmic Reticulum Vesicles, University of California Los Angeles, isotopic Studies on Structure-function Relationships of Nucleic Acids and Enzymes. Three Year Progress Report, May 1972 — October 1975, University of California Los Angeles, Energy Capture and Use in Plants and Bacteria. Final Technical Report, University of California Los Angeles, United States Department of Energy, Boyer Nobel Prize press release — The 1997 Nobel Prize in Chemistry UCLA webpage — Paul D
16.
Marshall Warren Nirenberg
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Marshall Warren Nirenberg was an American biochemist and geneticist. He shared a Nobel Prize in Physiology or Medicine in 1968 with Har Gobind Khorana and Robert W. Holley for breaking the genetic code, in the same year, together with Har Gobind Khorana, he was awarded the Louisa Gross Horwitz Prize from Columbia University. It was not known, however, how DNA directed the expression of proteins, Nirenberg teamed up with Heinrich J. Matthaei at the National Institutes of Health to answer these questions. They produced RNA composed solely of uracil, a nucleotide that only occurs in RNA and they then added this synthetic poly-uracil RNA into a cell-free extract of Escherichia coli which contained the DNA, RNA, ribosomes and other cellular machinery for protein synthesis. They added DNase, which breaks apart the DNA, so no additional proteins would be produced other than that from their synthetic RNA. They then added 1 radioactively labeled amino acid, the blocks of proteins. Only in the containing the radioactively labeled phenylalanine, was the resulting protein also radioactive. This implied that the code for phenylalanine on RNA consisted of a repetition of uracil bases. Indeed, as we now, it is UUU. This was the first step in deciphering the codons of the genetic code, in August 1961, at the International Congress of Biochemistry in Moscow, Nirenberg presented a paper to a small group of scientists. Francis Crick convinced the leaders to invite Nirenberg to repeat his performance the next day. Speaking before the congress of more than a thousand people. He quickly received great attention for these experiments. Within a few years, his team had performed similar experiments and found that three-base repeats of adenosine produced the amino acid lysine. The next breakthrough came when Philip Leder, a researcher in Nirenbergs lab. This greatly sped up the assignment of three-base codons to amino acids so that 50 codons were identified in this way, khoranas experiments confirmed these results and completed the genetic code translation. Faced with the possibility of helping the first NIH scientist win a Nobel prize, dr. DeWitt Stetten, Jr. director of the National Institute of Arthritis and Metabolic Diseases, called this period of collaboration NIHs finest hour. Nirenbergs later research focused on neuroscience, neural development, and the homeobox genes, Nirenberg was born in New York City, the son of Minerva and Harry Edward Nirenberg, a shirtmaker
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Frederic M. Richards
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He contributed many key experimental and theoretical results and developed new methods, garnering over 20,000 journal citations in several quite distinct research areas. He was elected to the National Academy of Sciences USA and the American Academy of Arts and Sciences, Richards was born on August 19,1925 in New York City to George H. Richards and Marianna Middlebrook Richards. Both parents were from old New England families who had settled in Fairfield and New London, the family usually spent summers in Connecticut, giving Richards an early affinity for the area which continued through his career at Yale University. He had two sisters, Marianna and Sarah. Marianna became a biochemist, and was a significant role model for Fred and this attitude played a strong role. In cementing our commitment to scientific careers and he learned glassblowing and electronics there, and tried to measure the universal gravitational constant using 100-pound cannonballs. With strong science interests, Richards thwarted his familys expectations by choosing MIT rather than Yale for college in 1943 and his undergraduate time was interrupted by two years in the army, which he described as uneventful. He then joined the Biochemistry department at Harvard Medical School and the lab of Barbara Low and she had worked with Dorothy Crowfoot Hodgkin to solve the x-ray crystal structure of penicillin, and was later active in protein crystallography. In 1954 he went to the Carlsberg Laboratory in Copenhagen to do research with Kaj Linderstrøm-Lang. In 1955 Richards joined the faculty at Yale University, where he stayed for the rest of his career, Richards was an avid and enthusiastic sailor. In addition to sailing on Long Island Sound, he voyaged north along the Canadian coast, south to Bermuda and he and his wife had sailboats and an outboard-motor utility boat known as Sallys Baage, which he had built himself. Chris Anfinsen, Richardss friend and his colleague as editors of Advances in Protein Chemistry and who recommended the Carlsberg Lab to him, was also an avid sailor and his sailing adventures included several transatlantic voyages. He was also an ice hockey player. Richards lived in Guilford, Connecticut, a town about 10 miles east of New Haven. Fred was married twice, to Heidi Clark Richards, daughter of biochemist Hans Clarke, and in 1959 to Sarah Wheatland Richards and he had three children – Sarah, Ruth, and George – and four grandchildren. His daughter Sarah described him as a lifelong scientist and sailor and his main loves were his scientific work which he finished at Yale University, sailing, working in his shop, and helping in the community. Fred and Sally were a presence in local land conservation efforts. He donated a 41-acre shoreline property to the Yale Peabody Museum Natural Areas, the property now has long-term protection for use in biological and geological research
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P. Roy Vagelos
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He attracted research scientists who developed many major new drugs. In addition to his business accomplishments, Vagelos is the author of more than 100 scientific papers, Vagelos grew up during the Depression as a son of Greek immigrants. He attended Rahway High School in his hometown of Rahway, New Jersey, after winning a partial scholarship, he left his familys small restaurant in Rahway, New Jersey, to become a doctor. He majored in chemistry at the University of Pennsylvania, graduating Phi Beta Kappa in 1950, Vagelos later earned an M. D. from Columbia University in 1954. Vagelos deferred military service while in school, but he was obligated to serve a two-year stint as an Army doctor. As a Columbia University College of Physicians and Surgeons trained surgeon and biochemist, for Vagelos, it was a fateful turning point. He was associated with Massachusetts General Hospital, Washington University and the Washington University School of Medicine before joining Merck, Sharp & Dohme Research Laboratories in Rahway. The author of more than 100 scientific papers, Vagelos has been elected to the American Academy of Arts and Sciences, the National Academy of Sciences, Vagelos donated over 15 million dollars to the University of Pennsylvania to create the Roy and Diana Vagelos Laboratories. These funds also made possible the founding the Vagelos Scholars Program In Molecular Life Sciences, later, he founded the Vagelos Integrated Program in Energy Research, supporting the necessity of energy research. In 1995, Vagelos received the NAS Award for Chemistry in Service to Society and was inducted into the Junior Achievement U. S. Business Hall of Fame. In 1999, he became a recipient of both the Bower Award for Business Leadership, as well as the Othmer Gold Medal, named the Roy and Diana Vagelos Education Center, it opened in August 2016. In 2013, Vagelos was invited to speak at the first annual Stony Brook University Research Your Future Symposium, in the mid-1980s, Merck & Co. discovered the drug ivermectin, capable of combatting the parasite that causes river blindness. At the time, the World Health Organization and the World Bank were conducting a campaign against the disease in West Africa. But the newly discovered drug was too expensive for those patients or their governments, over two decades, beginning in 1986, the drug reached more than 55 million people. The public health campaign was successful, and now river blindness is no longer a public health issue in the savannah areas of West Africa. How to Succeed The Future of the Pharmaceutical Industry, According to Roy Vagelos UPenn Honoree Appearances on C-SPAN Works by or about P. Roy Vagelos in libraries
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William J. Rutter
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William J. Rutter is an American biochemist who cofounded the early biotechnology company Chiron Corporation together with Edward Penhoet and Pablo DT Valenzuela. Rutter spent a time in the United States Navy and one year Brigham Young University. He earned an M. S. from University of Utah, between 1952 and 1968, Rutter held positions at the University of Wisconsin, the Karolinska Institutet, University of Illinois, Stanford University, and University of Washington. In 1969, he moved to the University of California, San Francisco, from 1983 until 1989, Rutter was Director of the Hormone Research Institute at UCSF. In 2003, William Rutter received the Biotechnology Heritage Award, William J. Rutter Papers, MSS 94-54, Archives & Special Collections, UCSF Library & CKM William J. Rutter – The Biotechnology Hall of Fame, Chemical Heritage Foundation
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Howard Martin Temin
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Howard Martin Temin was a U. S. geneticist and virologist. He discovered reverse transcriptase in the 1970s at the University of Wisconsin–Madison, for which he shared the 1975 Nobel Prize in Physiology or Medicine with Renato Dulbecco and David Baltimore. Temin was born in Philadelphia, Pennsylvania, to Jewish parents, Annette, an activist, and Henry Temin, as a high school student at Central High School in Pennsylvania, he participated in the Jackson Laboratorys Summer Student Program in Bar Harbor, Maine. The director of the program, C. C. ”Temin said that his experience at Jackson’s Laboratory is what really got him interested in science, Temin’s parents raised their family to have values associated with social justice and independent thinking, which was evident throughout his life. For Temin’s bar mitzvah, the donated money that would have been spent on the party. Temin was also the valedictorian of his class and he devoted his speech to relevant issues at the time including the recent hydrogen bomb activity and he received his bachelors degree from Swarthmore College in 1955 majoring and minoring in biology in the honors program. He received his degree in animal virology from the California Institute of Technology in 1959. Howard Temin’s first exposure to science was during his time at the California Institute of Technology as a graduate student in laboratory of Professor Renato Dulbecco. Temin originally studied embryology at CIT, but after about a year and he became interested Dulbecco’s lab after a chance run-in with Harry Rubin, a postdoctoral fellow in Dulbecco’s lab. In the lab, Temin studied the Rous sarcoma virus, a virus that infects chickens. As part of his thesis, Temin stated that the Rous Sarcoma Virus has “some kind of close relationship with the genome of the infected cell. Following receiving his doctorate, Temin continued to work in Dulbecco’s lab as a postdoctoral fellow. Even though Temin know he would be independent in Madison, because of the lack of research involving virology and oncology together, Temin stated that he was “supremely self-confident. ”When he first arrived in Madison in 1960. While studying the Rous sarcoma virus at UW-Madison, Temin began to refer to the material that the virus introduced to the cells, the “provirus. ”Using the antibiotic, actinomycin D. These results implied that the infecting Rous sarcoma virus was somehow generating complementary double-stranded DNA, temins description of how tumor viruses act on the genetic material of the cell through reverse transcription was revolutionary. Crick had claimed only that information cannot flow out of protein into DNA or RNA. Many highly respected scientists disregarded his work and declared it impossible, despite the lack of support from the scientific community, Temin continued to search for evidence to support his idea. In 1969, Temin and a fellow, Satoshi Mazutani
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Michael Stuart Brown
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Michael Stuart Brown is an American geneticist and Nobel laureate. He was awarded the Nobel Prize in Physiology or Medicine with Joseph L. Goldstein in 1985 for describing the regulation of cholesterol metabolism, Brown was born in Brooklyn, New York, the son of Evelyn, a homemaker, and Harvey Brown, a textile salesman. Brown graduated from the University of Pennsylvania in 1962 and received his M. D. from the University of Pennsylvania School of Medicine in 1966, the lack of sufficient LDL receptors is implicated in familial hypercholesterolemia, which predisposes heavily for cholesterol-related diseases. In addition to explaining the underlying pathology of disease, their work uncovered a fundamental aspect of cell biology - Receptor-mediated endocytosis. Their discoveries are improving more lives every year, both in the United States and around the world, New federal cholesterol guidelines will triple the number of Americans taking statin drugs to lower their cholesterol, reducing the risk of heart disease and stroke for countless people. Following these important advances, their team of dedicated researchers elucidated the role of lipid modification of proteins in cancer, in 1984 he was awarded the Louisa Gross Horwitz Prize from Columbia University together with Joseph L. Goldstein. In 1988, Brown received National Medal of Science for his contributions to the world of Medicine, in 1993, their trainees Xiaodong Wang and Michael Briggs purified the Sterol regulatory element binding proteins. He and his colleague are among the most highly cited scientists in the world, Brown is also on the prestigious Prix Galien USA Committee that recognizes the technical, scientific and clinical research skills necessary to develop innovative medicines. Brown has won awards and honors including
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Joseph L. Goldstein
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Joseph Leonard Goldstein is an American biochemist. He received the Nobel Prize in Physiology or Medicine in 1985, along with fellow University of Texas researcher, Michael Brown and their studies led to the development of statin drugs. Goldstein was born in Kingstree, South Carolina, the son of Fannie and Isadore E. Goldstein, Goldstein received his BSci from Washington and Lee University in 1962, and his MD from Texas Universitys Southwestern Medical School in 1966. Upon completion of his residency, Goldstein moved to the National Institutes of Health in Bethesda, Maryland, in 1972, Goldstein relocated back to the Southwestern Medical Center, accepting a post as the head of the Division of Medical Genetics. At the Southwestern Medical Center Goldstein collaborated extensively with Michael Brown, from 1973 to 1985, Goldstein and Brown together published over one hundred major papers. They are both listed in Thomson Reuters’ index of highly cited authors, frequently mentioned as a candidate for nationally-prominent positions in scientific administration, Goldstein, like his colleague Michael Brown, chose to continue hands-on research. In 1993, their trainees, Wang Xiaodong and Michael Briggs, purified the Sterol Regulatory Element-Binding Proteins. Goldstein is Chair, Molecular Genetics at University of Texas Southwestern Medical Center, together, Goldstein and Brown lead a research team that typically includes a dozen doctoral and postdoctoral trainees. They have trained over 145 graduate students and postdoctoral fellows, former postdoctoral fellow Thomas Südhof received the 2013 Nobel Prize in Medicine or Physiology and Helen H. Hobbs received the 2015 Breakthrough Prize in Life Sciences. Goldstein is a member of the U. S. National Academy of Sciences, Goldstein was appointed as Chairman of the Albert Lasker Medical Research Awards jury in 1995, and was a recipient of the award ten years earlier. Since 2000, Goldstein has authored a series of essays on the relationship between art and science that appear in the annual Nature Medicine supplement that accompanies the Lasker Awards. He also serves as Chairman of the Board of Scientific Counselors of the Broad Institute and he previously served on The Board of Scientific Governors of the Scripps Research Institute, a nonprofit institute that conducts biomedical research. Joseph L. Goldstein has been awarded the following, Since 2000, Goldstein has authored a series of essays considering science as a creative pursuit, and explores the links between the art and science. The essays appear in the journal Nature Medicine, and coincide with the announcement of the Lasker Awards
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Paul Schimmel
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Paul Reinhard Schimmel is an American biophysical chemist and translational medicine pioneer. Paul Schimmel was born in Hartford, Connecticut and he is Ernest and Jean Hahn Professor at the Skaggs Institute for Chemical Biology at The Scripps Research Institute. For his entire career Schimmel’s research focused on a group of enzymes known as aminoacyl tRNA synthetases. The synthetases are believed by many to be among the first enzymes to arise on this planet in the stages of the evolution of life. These enzymes translate the information in all living organisms. In each cell, there is a separate tRNA synthetase for each of the 20 amino acids, in translating, or interpreting, the genetic material, they catalyze reactions whereby each amino acid is matched with a nucleotide triplet embedded in its cognate tRNA. In this way, the tRNA synthetases establish the rules of the code and, because of this role. Because of decades of research of Schimmel and others, this group of enzymes is now understood to have novel functions. Schimmel and his wife Cleo have two daughters and eight grandchildren, Schimmel’s laboratory discovered a universal mechanism for correcting errors in the translation of the genetic material. This mechanism is regarded as one of the most fundamental in biology, specifically, they discovered an activity in aminoacyl tRNA synthetases that removes an amino acid that has been charged to the wrong tRNA. He later discovered the novel module in synthetases that encodes this deacylase activity and these error correction activities were shown to be intimately associated with the beginnings of living organisms. Schimmel’s laboratory discovered what has been referred to as a “second genetic code” that relates specific atomic determinants in small RNA substrates to specific aminoacylation and this RNA code is considered to give critical insights into the development of the modern genetic code and protein synthesis. Schimmel and coworkers were among the first to use methods to establish the modular design of proteins in general. ESTs provide a way to all genes that are expressed in a specific tissue, such as muscle. Nature magazine listed Schimmel’s work on ESTs as one of the four key developments that launched the human genome project and this work led to efforts to commercialize applications of human synthetases to treat diseases. Assistant Professor of Biology and Chemistry, MIT, 1967-71, associate Professor of Biology and Chemistry, MIT, 1971-76. Visiting Scientist, Department of Biological Sciences, University of California, Santa Barbara, Professor of Biochemistry and Biophysics, MIT, 1976–1992. John D. and Catherine T. MacArthur Professor of Biochemistry and Biophysics, MIT, Professor and Member, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 1997–2000
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Thomas A. Steitz
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Steitz was awarded the 2009 Nobel Prize in Chemistry along with Venkatraman Ramakrishnan and Ada Yonath for studies of the structure and function of the ribosome. Born in Milwaukee, Wisconsin, Steitz studied chemistry as an undergraduate at Lawrence University in Appleton, Wisconsin, while there he was a member of the fraternity, Delta Tau Delta, the Delta Nu chapter. In June 2010, the University renamed its chemistry building Thomas A. Steitz Hall of Science, Steitz joined the Yale faculty in 1970, where he continued to work on cellular and structural biology. Steitz and Peter Moore determined the structure of the large 50S ribosomal subunit using X-ray crystallography. In 2009, Steitz was awarded the Nobel Prize in Chemistry for his ribosome research and he was also a Macy Fellow at the University of Göttingen during 1976–1977 and a Fairchild Scholar at the California Institute of Technology during 1984-1985. Nobel Prize in Chemistry Elected a Foreign Member of the Royal Society in 2011 He is married to Joan A. Steitz, also a Sterling Professor of Molecular Biophysics and they live in Branford, Connecticut and have one son, Jon. Determination of the Atomic-Resolution Crystal Structure of the Large Subunit from the Ribosome of Haloarcula marismortui, the Atomic Resolution Crystal Structure of the Large Ribosomal Subunit from Haloarcula marismortui, NSLS Activity Report. Thomas Steitz - MIPtalk. com interview http, //blogs. lawrence. edu/news/2009/10/lawrence_university_graduate_a. html
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Thomas Cech
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Thomas Robert Cech is an American chemist who shared the 1989 Nobel Prize in Chemistry with Sidney Altman, for their discovery of the catalytic properties of RNA. Cech discovered that RNA could itself cut strands of RNA, which showed life could have started as RNA. He also studied telomeres, and his lab discovered an enzyme, TERT, as president of Howard Hughes Medical Institute, he promoted science education, and he teaches an undergraduate chemistry course at the University of Colorado. Cech was born to parents of Czech origin in Chicago, he grew up in Iowa City, in junior high school, he knocked on the doors of geology professors at the University of Iowa, and asked them to discuss crystal structures, meteorites and fossils. In 1966, he entered Grinnell College where he studied Homers Odyssey, Dantes Inferno and he married his organic chemistry lab partner, Carol Lynn Martinson, and graduated with a B. A. in 1970. In 2000, Cech succeeded Purnell Choppin as president of the Howard Hughes Medical Institute in Maryland and he also continues to head his biochemistry laboratory, the Colorado Initiative in Molecular Biotechnology, at the University of Colorado, Boulder. Cech continues to teach chemistry at CU-Boulder. On April 1,2008, Cech announced that he would step down as the president of HHMI, to return to teaching and research, Cechs main research area is that of the process of transcription in the nucleus of cells. He studies how the code of DNA is transcribed into RNA. In the 1970s, Cech had been studying the splicing of RNA in the unicellular organism Tetrahymena thermophila when he discovered that an unprocessed RNA molecule could splice itself, rNA-processing reactions and protein synthesis on ribosomes in particular are catalysed by RNA. RNA enzymes are known as ribozymes and have provided a new tool for gene technology and they also have the potential to provide new therapeutic agents – for example, they have the ability to destroy and cleave invading, viral RNAs. Cechs second area of research is on telomeres, the structure that protects the ends of chromosomes, telomeres are shortened with every duplication of DNA, and must be lengthened again. He studies telomerase, the enzyme that copies the telomeric sequences, the active site protein subunits of telomerase comprise a new class of reverse transcriptases, enzymes previously thought to be restricted to viruses and transposable elements. Telomerase is activated in 90% of human cancers, therefore, a drug that would inhibit its activity could be useful in treating cancer. In 1987, Cech was elected to the United States National Academy of Sciences and in 1988 he was elected to the American Academy of Arts, in 2007, he received the Othmer Gold Medal for outstanding contributions to progress in chemistry and science. History of RNA biology List of RNA biologists Tom Cechs short talk, Discovering Ribozymes Chemical and Engineering News The Nobel Prize in Chemistry 1989, Sidney Altman, Thomas R
26.
Michael H. Gelb
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Professor Michael H. Gelb is an American biochemist and chemist specializing in enzymes and particularly those of medical significance. He is the Harry and Catherine Jaynne Boand Endowed Professor of Chemistry and Biochemistry at the University of Washington in Seattle and he also teaches Honors Organic Chemistry, Chemical Biology and Enzymology. Gelb studied chemistry and biochemistry at the University of California, Davis before taking a Ph. D under Stephen G. Sligar at Yale University on aspects of the mechanism of cytochrome P450. Since 1985 Gelb has been a faculty member at the University of Washington in the Departments of Chemistry and Biochemistry, the Gelb laboratory uses a number of techniques in molecular and cellular biochemistry as well as synthetic organic chemistry to study enzymatic processes of biomedical significance. Routine newborn screening of lysosomal storage diseases using technology developed in the Gelb laboratory was brought into use in New York state in 2006, plans are underway to expand screening in other regions of the USA and in several other countries. Pfizer Award in Enzyme Chemistry from the American Chemical Society, ICI Pharmaceuticals Award for Excellence in Chemistry. In his spare time, Gelb enjoys surfing, playing classical guitar, the Gelb lab website at the University of Washington
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Gerald Joyce
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Joyce received his Bachelor of Arts from the University of Chicago in 1978, completed his M. D. and Ph. D. at the University of California, San Diego in 1984. He was a fellow and senior research associate at the Salk Institute from 1985 to 1989. Joyce was elected to the U. S. National Academy of Sciences in 2001 and he served as Dean of the Faculty at Scripps from 2006 to 2011, during which time he was instrumental in founding a second campus in Jupiter, Florida. He was elected to the American Academy of Arts & Sciences in 2011 and he is currently the director of GNF and the chair of the JASON advisory group, which he joined in 1996. Joyce received the Urey medal of the International Society for the Study of the Origin of Life in 2005, in 2009, Joyces lab was the first to produce a self-replicating in vitro system, capable of exponential growth and continuing evolution, composed entirely of RNA enzymes. NAS Award in Molecular Biology,1994 Pfizer Award in Enzyme Chemistry,1995 Herbert W. Dickerman Award,1997 Hans Sigrist Prize,1997 H
