Nobel Prize Signed Sketch Autographs Split Genes Chemistry Roberts Olah Wow

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Seller: memorabilia111 ✉️ (808) 100%, Location: Ann Arbor, Michigan, US, Ships to: US & many other countries, Item: 176277810595 NOBEL PRIZE SIGNED SKETCH AUTOGRAPHS SPLIT GENES CHEMISTRY ROBERTS OLAH WOW. NOBEL PRIZE WINNER GEORGE A. OLAH WINNER FOR NOBEL PRIZE IN CHEMCISTRY 1994 QUOTE SIGNED ON 4X6 CARD AND SKETCH ON 3X5 CARD BY RICHARD ROBERTSS NOBEL PRIZE WINNER FOR SPLITTING GENES Sir Richard John Roberts FRS (born 6 September 1943) is a British biochemist and molecular biologist. He was awarded the 1993 Nobel Prize in Physiology or Medicine with Phillip Allen Sharp for the discovery of introns in eukaryotic DNA and the mechanism of gene-splicing. He currently works at New England Biolabs George Andrew Olah was a Hungarian-American chemist. His research involved the generation and reactivity of carbocations via superacids. For this research, Olah was awarded a Nobel Prize in Chemistry in 1994 "for his contribution to carbocation chemistry."

Sir Richard John Roberts FRS[5] (born 6 September 1943) is a British biochemist and molecular biologist. He was awarded the 1993 Nobel Prize in Physiology or Medicine with Phillip Allen Sharp for the discovery of introns in eukaryotic DNA and the mechanism of gene-splicing. He currently works at New England Biolabs.[10][11][12] Early life and education Roberts was born in Derby, the son of Edna (Allsop) and John Roberts, an auto mechanic.[8] When he was four, Roberts' family moved to Bath. In Bath, he attended City of Bath Boys' School.[8] As a child he at first wanted to be a detective and then, when given a chemistry set, a chemist. In 1965 he graduated from the University of Sheffield with a Bachelor of Science degree in Chemistry followed by a PhD in 1969.[4] His thesis involved phytochemical studies of neoflavonoids and isoflavonoids.[1][13] Career and research During 1969–1972, he did postdoctoral research at Harvard University.[8] before moving to Cold Spring Harbor Laboratory,[14] where he was hired by James Dewey Watson, a co-discoverer of the structure of DNA and a fellow Nobel laureate. In this period he also visited the MRC Laboratory of Molecular Biology for the first time, working alongside Fred Sanger.[15] In 1977, he published his discovery of RNA splicing.[14] In 1992, he moved to New England Biolabs.[8] The following year, he shared a Nobel Prize with his former colleague at Cold Spring Harbor Phillip Allen Sharp.[16] Roberts's discovery of the alternative splicing of genes, in particular, has had a profound impact on the study and applications of molecular biology.[5] The realisation that individual genes could exist as separate, disconnected segments within longer strands of DNA first arose in his 1977 study of adenovirus,[14] one of the viruses responsible for causing the common cold. Robert's research in this field resulted in a fundamental shift in our understanding of genetics, and has led to the discovery of split genes in higher organisms, including human beings.[5][12] Awards and honours In 1992, Roberts received an honorary doctorate from the Faculty of Medicine at Uppsala University, Sweden.[17] After becoming a Nobel laureate in 1993 he was awarded an Honorary Degree (Doctor of Science) by the University of Bath in 1994.[18] Roberts also received the Golden Plate Award of the American Academy of Achievement in 1994.[19] In 2021 he was awarded the Lomonosov Gold Medal of the Russian Academy of Sciences.[20] Roberts was elected a Fellow of the Royal Society (FRS) in 1995[5] and a member of the European Molecular Biology Organization (EMBO) in the same year.[6] In 2005, a multimillion-pound expansion to the chemistry department at the University of Sheffield, where he had been a student, was named after him. A refurbished science department at Beechen Cliff School (previously City of Bath Boys' School) was also named after Roberts, who had donated a substantial sum of his Nobel prize winnings to the school.[21] Roberts is an atheist and was one of the signers of the Humanist Manifesto.[22][23] He was knighted in the 2008 Birthday Honours. Roberts is a member of the Advisory Board of Patient Innovation,[24] a nonprofit, international, multilingual, free venue for patients and caregivers of any disease to share their innovations. Roberts has been a keynote speaker at the Congress of Future Medical Leaders (2014, 2015, 2016, 2020).[25] He also is the chairman of The Laureate Science Alliance, a non-profit supporting research worldwide. In 2016, Roberts and other Nobelists composed and signed a "Laureates Letter Supporting Precision Agriculture (GMOs)" addressed to the leaders of Greenpeace, the United Nations and global governments and Sir Roberts has advocated for Genetically Modified Organisms (GMOs) in general and Golden Rice in particular to advance health in developing countries, noting the high safety record of GM foods.[26][27] Genetic engineering, also called genetic modification or genetic manipulation, is the modification and manipulation of an organism's genes using technology. It is a set of technologies used to change the genetic makeup of cells, including the transfer of genes within and across species boundaries to produce improved or novel organisms. New DNA is obtained by either isolating and copying the genetic material of interest using recombinant DNA methods or by artificially synthesising the DNA. A construct is usually created and used to insert this DNA into the host organism. The first recombinant DNA molecule was made by Paul Berg in 1972 by combining DNA from the monkey virus SV40 with the lambda virus. As well as inserting genes, the process can be used to remove, or "knock out", genes. The new DNA can be inserted randomly, or targeted to a specific part of the genome.[1] An organism that is generated through genetic engineering is considered to be genetically modified (GM) and the resulting entity is a genetically modified organism (GMO). The first GMO was a bacterium generated by Herbert Boyer and Stanley Cohen in 1973. Rudolf Jaenisch created the first GM animal when he inserted foreign DNA into a mouse in 1974. The first company to focus on genetic engineering, Genentech, was founded in 1976 and started the production of human proteins. Genetically engineered human insulin was produced in 1978 and insulin-producing bacteria were commercialised in 1982. Genetically modified food has been sold since 1994, with the release of the Flavr Savr tomato. The Flavr Savr was engineered to have a longer shelf life, but most current GM crops are modified to increase resistance to insects and herbicides. GloFish, the first GMO designed as a pet, was sold in the United States in December 2003. In 2016 salmon modified with a growth hormone were sold. Genetic engineering has been applied in numerous fields including research, medicine, industrial biotechnology and agriculture. In research, GMOs are used to study gene function and expression through loss of function, gain of function, tracking and expression experiments. By knocking out genes responsible for certain conditions it is possible to create animal model organisms of human diseases. As well as producing hormones, vaccines and other drugs, genetic engineering has the potential to cure genetic diseases through gene therapy. The same techniques that are used to produce drugs can also have industrial applications such as producing enzymes for laundry detergent, cheeses and other products. The rise of commercialised genetically modified crops has provided economic benefit to farmers in many different countries, but has also been the source of most of the controversy surrounding the technology. This has been present since its early use; the first field trials were destroyed by anti-GM activists. Although there is a scientific consensus that currently available food derived from GM crops poses no greater risk to human health than conventional food, critics consider GM food safety a leading concern. Gene flow, impact on non-target organisms, control of the food supply and intellectual property rights have also been raised as potential issues. These concerns have led to the development of a regulatory framework, which started in 1975. It has led to an international treaty, the Cartagena Protocol on Biosafety, that was adopted in 2000. Individual countries have developed their own regulatory systems regarding GMOs, with the most marked differences occurring between the US and Europe. IUPAC definition Genetic engineering: Process of inserting new genetic information into existing cells in order to modify a specific organism for the purpose of changing its characteristics. Note: Adapted from ref.[2][3] Overview Comparison of conventional plant breeding with transgenic and cisgenic genetic modification Genetic engineering is a process that alters the genetic structure of an organism by either removing or introducing DNA, or modifying existing genetic material in situ. Unlike traditional animal and plant breeding, which involves doing multiple crosses and then selecting for the organism with the desired phenotype, genetic engineering takes the gene directly from one organism and delivers it to the other. This is much faster, can be used to insert any genes from any organism (even ones from different domains) and prevents other undesirable genes from also being added.[4] Genetic engineering could potentially fix severe genetic disorders in humans by replacing the defective gene with a functioning one.[5] It is an important tool in research that allows the function of specific genes to be studied.[6] Drugs, vaccines and other products have been harvested from organisms engineered to produce them.[7] Crops have been developed that aid food security by increasing yield, nutritional value and tolerance to environmental stresses.[8] The DNA can be introduced directly into the host organism or into a cell that is then fused or hybridised with the host.[9] This relies on recombinant nucleic acid techniques to form new combinations of heritable genetic material followed by the incorporation of that material either indirectly through a vector system or directly through micro-injection, macro-injection or micro-encapsulation. Genetic engineering does not normally include traditional breeding, in vitro fertilisation, induction of polyploidy, mutagenesis and cell fusion techniques that do not use recombinant nucleic acids or a genetically modified organism in the process.[9] However, some broad definitions of genetic engineering include selective breeding.[10] Cloning and stem cell research, although not considered genetic engineering,[11] are closely related and genetic engineering can be used within them.[12] Synthetic biology is an emerging discipline that takes genetic engineering a step further by introducing artificially synthesised material into an organism.[13] Plants, animals or microorganisms that have been changed through genetic engineering are termed genetically modified organisms or GMOs.[14] If genetic material from another species is added to the host, the resulting organism is called transgenic. If genetic material from the same species or a species that can naturally breed with the host is used the resulting organism is called cisgenic.[15] If genetic engineering is used to remove genetic material from the target organism the resulting organism is termed a knockout organism.[16] In Europe genetic modification is synonymous with genetic engineering while within the United States of America and Canada genetic modification can also be used to refer to more conventional breeding methods.[17][18][19] History Main article: History of genetic engineering Humans have altered the genomes of species for thousands of years through selective breeding, or artificial selection[20]: 1 [21]: 1  as contrasted with natural selection. More recently, mutation breeding has used exposure to chemicals or radiation to produce a high frequency of random mutations, for selective breeding purposes. Genetic engineering as the direct manipulation of DNA by humans outside breeding and mutations has only existed since the 1970s. The term "genetic engineering" was first coined by Jack Williamson in his science fiction novel Dragon's Island, published in 1951[22] – one year before DNA's role in heredity was confirmed by Alfred Hershey and Martha Chase,[23] and two years before James Watson and Francis Crick showed that the DNA molecule has a double-helix structure – though the general concept of direct genetic manipulation was explored in rudimentary form in Stanley G. Weinbaum's 1936 science fiction story Proteus Island.[24][25] In 1974 Rudolf Jaenisch created a genetically modified mouse, the first GM animal. In 1972, Paul Berg created the first recombinant DNA molecules by combining DNA from the monkey virus SV40 with that of the lambda virus.[26] In 1973 Herbert Boyer and Stanley Cohen created the first transgenic organism by inserting antibiotic resistance genes into the plasmid of an Escherichia coli bacterium.[27][28] A year later Rudolf Jaenisch created a transgenic mouse by introducing foreign DNA into its embryo, making it the world's first transgenic animal[29] These achievements led to concerns in the scientific community about potential risks from genetic engineering, which were first discussed in depth at the Asilomar Conference in 1975. One of the main recommendations from this meeting was that government oversight of recombinant DNA research should be established until the technology was deemed safe.[30][31] In 1976 Genentech, the first genetic engineering company, was founded by Herbert Boyer and Robert Swanson and a year later the company produced a human protein (somatostatin) in E. coli. Genentech announced the production of genetically engineered human insulin in 1978.[32] In 1980, the U.S. Supreme Court in the Diamond v. Chakrabarty case ruled that genetically altered life could be patented.[33] The insulin produced by bacteria was approved for release by the Food and Drug Administration (FDA) in 1982.[34] In 1983, a biotech company, Advanced Genetic Sciences (AGS) applied for U.S. government authorisation to perform field tests with the ice-minus strain of Pseudomonas syringae to protect crops from frost, but environmental groups and protestors delayed the field tests for four years with legal challenges.[35] In 1987, the ice-minus strain of P. syringae became the first genetically modified organism (GMO) to be released into the environment[36] when a strawberry field and a potato field in California were sprayed with it.[37] Both test fields were attacked by activist groups the night before the tests occurred: "The world's first trial site attracted the world's first field trasher".[36] The first field trials of genetically engineered plants occurred in France and the US in 1986, tobacco plants were engineered to be resistant to herbicides.[38] The People's Republic of China was the first country to commercialise transgenic plants, introducing a virus-resistant tobacco in 1992.[39] In 1994 Calgene attained approval to commercially release the first genetically modified food, the Flavr Savr, a tomato engineered to have a longer shelf life.[40] In 1994, the European Union approved tobacco engineered to be resistant to the herbicide bromoxynil, making it the first genetically engineered crop commercialised in Europe.[41] In 1995, Bt potato was approved safe by the Environmental Protection Agency, after having been approved by the FDA, making it the first pesticide producing crop to be approved in the US.[42] In 2009 11 transgenic crops were grown commercially in 25 countries, the largest of which by area grown were the US, Brazil, Argentina, India, Canada, China, Paraguay and South Africa.[43] In 2010, scientists at the J. Craig Venter Institute created the first synthetic genome and inserted it into an empty bacterial cell. The resulting bacterium, named Mycoplasma laboratorium, could replicate and produce proteins.[44][45] Four years later this was taken a step further when a bacterium was developed that replicated a plasmid containing a unique base pair, creating the first organism engineered to use an expanded genetic alphabet.[46][47] In 2012, Jennifer Doudna and Emmanuelle Charpentier collaborated to develop the CRISPR/Cas9 system,[48][49] a technique which can be used to easily and specifically alter the genome of almost any organism.[50] Process Main article: Genetic engineering techniques Polymerase chain reaction is a powerful tool used in molecular cloning. Creating a GMO is a multi-step process. Genetic engineers must first choose what gene they wish to insert into the organism. This is driven by what the aim is for the resultant organism and is built on earlier research. Genetic screens can be carried out to determine potential genes and further tests then used to identify the best candidates. The development of microarrays, transcriptomics and genome sequencing has made it much easier to find suitable genes.[51] Luck also plays its part; the Roundup Ready gene was discovered after scientists noticed a bacterium thriving in the presence of the herbicide.[52] Gene isolation and cloning Main article: Molecular cloning The next step is to isolate the candidate gene. The cell containing the gene is opened and the DNA is purified.[53] The gene is separated by using restriction enzymes to cut the DNA into fragments[54] or polymerase chain reaction (PCR) to amplify up the gene segment.[55] These segments can then be extracted through gel electrophoresis. If the chosen gene or the donor organism's genome has been well studied it may already be accessible from a genetic library. If the DNA sequence is known, but no copies of the gene are available, it can also be artificially synthesised.[56] Once isolated the gene is ligated into a plasmid that is then inserted into a bacterium. The plasmid is replicated when the bacteria divide, ensuring unlimited copies of the gene are available.[57] The RK2 plasmid is notable for its ability to replicate in a wide variety of single-celled organisms, which makes it suitable as a genetic engineering tool.[58] Before the gene is inserted into the target organism it must be combined with other genetic elements. These include a promoter and terminator region, which initiate and end transcription. A selectable marker gene is added, which in most cases confers antibiotic resistance, so researchers can easily determine which cells have been successfully transformed. The gene can also be modified at this stage for better expression or effectiveness. These manipulations are carried out using recombinant DNA techniques, such as restriction digests, ligations and molecular cloning.[59] Inserting DNA into the host genome Main article: Gene delivery A gene gun uses biolistics to insert DNA into plant tissue. There are a number of techniques used to insert genetic material into the host genome. Some bacteria can naturally take up foreign DNA. This ability can be induced in other bacteria via stress (e.g. thermal or electric shock), which increases the cell membrane's permeability to DNA; up-taken DNA can either integrate with the genome or exist as extrachromosomal DNA. DNA is generally inserted into animal cells using microinjection, where it can be injected through the cell's nuclear envelope directly into the nucleus, or through the use of viral vectors.[60] Plant genomes can be engineered by physical methods or by use of Agrobacterium for the delivery of sequences hosted in T-DNA binary vectors. In plants the DNA is often inserted using Agrobacterium-mediated transformation,[61] taking advantage of the Agrobacteriums T-DNA sequence that allows natural insertion of genetic material into plant cells.[62] Other methods include biolistics, where particles of gold or tungsten are coated with DNA and then shot into young plant cells,[63] and electroporation, which involves using an electric shock to make the cell membrane permeable to plasmid DNA. As only a single cell is transformed with genetic material, the organism must be regenerated from that single cell. In plants this is accomplished through the use of tissue culture.[64][65] In animals it is necessary to ensure that the inserted DNA is present in the embryonic stem cells.[66] Bacteria consist of a single cell and reproduce clonally so regeneration is not necessary. Selectable markers are used to easily differentiate transformed from untransformed cells. These markers are usually present in the transgenic organism, although a number of strategies have been developed that can remove the selectable marker from the mature transgenic plant.[67] A. tumefaciens attaching itself to a carrot cell Further testing using PCR, Southern hybridization, and DNA sequencing is conducted to confirm that an organism contains the new gene.[68] These tests can also confirm the chromosomal location and copy number of the inserted gene. The presence of the gene does not guarantee it will be expressed at appropriate levels in the target tissue so methods that look for and measure the gene products (RNA and protein) are also used. These include northern hybridisation, quantitative RT-PCR, Western blot, immunofluorescence, ELISA and phenotypic analysis.[69] The new genetic material can be inserted randomly within the host genome or targeted to a specific location. The technique of gene targeting uses homologous recombination to make desired changes to a specific endogenous gene. This tends to occur at a relatively low frequency in plants and animals and generally requires the use of selectable markers. The frequency of gene targeting can be greatly enhanced through genome editing. Genome editing uses artificially engineered nucleases that create specific double-stranded breaks at desired locations in the genome, and use the cell's endogenous mechanisms to repair the induced break by the natural processes of homologous recombination and nonhomologous end-joining. There are four families of engineered nucleases: meganucleases,[70][71] zinc finger nucleases,[72][73] transcription activator-like effector nucleases (TALENs),[74][75] and the Cas9-guideRNA system (adapted from CRISPR).[76][77] TALEN and CRISPR are the two most commonly used and each has its own advantages.[78] TALENs have greater target specificity, while CRISPR is easier to design and more efficient.[78] In addition to enhancing gene targeting, engineered nucleases can be used to introduce mutations at endogenous genes that generate a gene knockout.[79][80] Applications Genetic engineering has applications in medicine, research, industry and agriculture and can be used on a wide range of plants, animals and microorganisms. Bacteria, the first organisms to be genetically modified, can have plasmid DNA inserted containing new genes that code for medicines or enzymes that process food and other substrates.[81][82] Plants have been modified for insect protection, herbicide resistance, virus resistance, enhanced nutrition, tolerance to environmental pressures and the production of edible vaccines.[83] Most commercialised GMOs are insect resistant or herbicide tolerant crop plants.[84] Genetically modified animals have been used for research, model animals and the production of agricultural or pharmaceutical products. The genetically modified animals include animals with genes knocked out, increased susceptibility to disease, hormones for extra growth and the ability to express proteins in their milk.[85] Medicine Genetic engineering has many applications to medicine that include the manufacturing of drugs, creation of model animals that mimic human conditions and gene therapy. One of the earliest uses of genetic engineering was to mass-produce human insulin in bacteria.[32] This application has now been applied to human growth hormones, follicle stimulating hormones (for treating infertility), human albumin, monoclonal antibodies, antihemophilic factors, vaccines and many other drugs.[86][87] Mouse hybridomas, cells fused together to create monoclonal antibodies, have been adapted through genetic engineering to create human monoclonal antibodies.[88] Genetically engineered viruses are being developed that can still confer immunity, but lack the infectious sequences.[89] Genetic engineering is also used to create animal models of human diseases. Genetically modified mice are the most common genetically engineered animal model.[90] They have been used to study and model cancer (the oncomouse), obesity, heart disease, diabetes, arthritis, substance abuse, anxiety, aging and Parkinson disease.[91] Potential cures can be tested against these mouse models. Gene therapy is the genetic engineering of humans, generally by replacing defective genes with effective ones. Clinical research using somatic gene therapy has been conducted with several diseases, including X-linked SCID,[92] chronic lymphocytic leukemia (CLL),[93][94] and Parkinson's disease.[95] In 2012, Alipogene tiparvovec became the first gene therapy treatment to be approved for clinical use.[96][97] In 2015 a virus was used to insert a healthy gene into the skin cells of a boy suffering from a rare skin disease, epidermolysis bullosa, in order to grow, and then graft healthy skin onto 80 percent of the boy's body which was affected by the illness.[98] Germline gene therapy would result in any change being inheritable, which has raised concerns within the scientific community.[99][100] In 2015, CRISPR was used to edit the DNA of non-viable human embryos,[101][102] leading scientists of major world academies to call for a moratorium on inheritable human genome edits.[103] There are also concerns that the technology could be used not just for treatment, but for enhancement, modification or alteration of a human beings' appearance, adaptability, intelligence, character or behavior.[104] The distinction between cure and enhancement can also be difficult to establish.[105] In November 2018, He Jiankui announced that he had edited the genomes of two human embryos, to attempt to disable the CCR5 gene, which codes for a receptor that HIV uses to enter cells. The work was widely condemned as unethical, dangerous, and premature.[106] Currently, germline modification is banned in 40 countries. Scientists that do this type of research will often let embryos grow for a few days without allowing it to develop into a baby.[107] Researchers are altering the genome of pigs to induce the growth of human organs, with the aim of increasing the success of pig to human organ transplantation.[108] Scientists are creating "gene drives", changing the genomes of mosquitoes to make them immune to malaria, and then looking to spread the genetically altered mosquitoes throughout the mosquito population in the hopes of eliminating the disease.[109] Research Knockout mice Human cells in which some proteins are fused with green fluorescent protein to allow them to be visualised Genetic engineering is an important tool for natural scientists, with the creation of transgenic organisms one of the most important tools for analysis of gene function.[110] Genes and other genetic information from a wide range of organisms can be inserted into bacteria for storage and modification, creating genetically modified bacteria in the process. Bacteria are cheap, easy to grow, clonal, multiply quickly, relatively easy to transform and can be stored at -80 °C almost indefinitely. Once a gene is isolated it can be stored inside the bacteria providing an unlimited supply for research.[111] Organisms are genetically engineered to discover the functions of certain genes. This could be the effect on the phenotype of the organism, where the gene is expressed or what other genes it interacts with. These experiments generally involve loss of function, gain of function, tracking and expression. Loss of function experiments, such as in a gene knockout experiment, in which an organism is engineered to lack the activity of one or more genes. In a simple knockout a copy of the desired gene has been altered to make it non-functional. Embryonic stem cells incorporate the altered gene, which replaces the already present functional copy. These stem cells are injected into blastocysts, which are implanted into surrogate mothers. This allows the experimenter to analyse the defects caused by this mutation and thereby determine the role of particular genes. It is used especially frequently in developmental biology.[112] When this is done by creating a library of genes with point mutations at every position in the area of interest, or even every position in the whole gene, this is called "scanning mutagenesis". The simplest method, and the first to be used, is "alanine scanning", where every position in turn is mutated to the unreactive amino acid alanine.[113] Gain of function experiments, the logical counterpart of knockouts. These are sometimes performed in conjunction with knockout experiments to more finely establish the function of the desired gene. The process is much the same as that in knockout engineering, except that the construct is designed to increase the function of the gene, usually by providing extra copies of the gene or inducing synthesis of the protein more frequently. Gain of function is used to tell whether or not a protein is sufficient for a function, but does not always mean it is required, especially when dealing with genetic or functional redundancy.[112] Tracking experiments, which seek to gain information about the localisation and interaction of the desired protein. One way to do this is to replace the wild-type gene with a 'fusion' gene, which is a juxtaposition of the wild-type gene with a reporting element such as green fluorescent protein (GFP) that will allow easy visualisation of the products of the genetic modification. While this is a useful technique, the manipulation can destroy the function of the gene, creating secondary effects and possibly calling into question the results of the experiment. More sophisticated techniques are now in development that can track protein products without mitigating their function, such as the addition of small sequences that will serve as binding motifs to monoclonal antibodies.[112] Expression studies aim to discover where and when specific proteins are produced. In these experiments, the DNA sequence before the DNA that codes for a protein, known as a gene's promoter, is reintroduced into an organism with the protein coding region replaced by a reporter gene such as GFP or an enzyme that catalyses the production of a dye. Thus the time and place where a particular protein is produced can be observed. Expression studies can be taken a step further by altering the promoter to find which pieces are crucial for the proper expression of the gene and are actually bound by transcription factor proteins; this process is known as promoter bashing.[114] Industrial Main article: Industrial microbiology Products of genetic engineering Organisms can have their cells transformed with a gene coding for a useful protein, such as an enzyme, so that they will overexpress the desired protein. Mass quantities of the protein can then be manufactured by growing the transformed organism in bioreactor equipment using industrial fermentation, and then purifying the protein.[115] Some genes do not work well in bacteria, so yeast, insect cells or mammalian cells can also be used.[116] These techniques are used to produce medicines such as insulin, human growth hormone, and vaccines, supplements such as tryptophan, aid in the production of food (chymosin in cheese making) and fuels.[117] Other applications with genetically engineered bacteria could involve making them perform tasks outside their natural cycle, such as making biofuels,[118] cleaning up oil spills, carbon and other toxic waste[119] and detecting arsenic in drinking water.[120] Certain genetically modified microbes can also be used in biomining and bioremediation, due to their ability to extract heavy metals from their environment and incorporate them into compounds that are more easily recoverable.[121] In materials science, a genetically modified virus has been used in a research laboratory as a scaffold for assembling a more environmentally friendly lithium-ion battery.[122][123] Bacteria have also been engineered to function as sensors by expressing a fluorescent protein under certain environmental conditions.[124] Agriculture Main articles: Genetically modified crops and Genetically modified food Bt-toxins present in peanut leaves (bottom image) protect it from extensive damage caused by lesser cornstalk borer larvae (top image).[125] One of the best-known and controversial applications of genetic engineering is the creation and use of genetically modified crops or genetically modified livestock to produce genetically modified food. Crops have been developed to increase production, increase tolerance to abiotic stresses, alter the composition of the food, or to produce novel products.[126] The first crops to be released commercially on a large scale provided protection from insect pests or tolerance to herbicides. Fungal and virus resistant crops have also been developed or are in development.[127][128] This makes the insect and weed management of crops easier and can indirectly increase crop yield.[129][130] GM crops that directly improve yield by accelerating growth or making the plant more hardy (by improving salt, cold or drought tolerance) are also under development.[131] In 2016 Salmon have been genetically modified with growth hormones to reach normal adult size much faster.[132] GMOs have been developed that modify the quality of produce by increasing the nutritional value or providing more industrially useful qualities or quantities.[131] The Amflora potato produces a more industrially useful blend of starches. Soybeans and canola have been genetically modified to produce more healthy oils.[133][134] The first commercialised GM food was a tomato that had delayed ripening, increasing its shelf life.[135] Plants and animals have been engineered to produce materials they do not normally make. Pharming uses crops and animals as bioreactors to produce vaccines, drug intermediates, or the drugs themselves; the useful product is purified from the harvest and then used in the standard pharmaceutical production process.[136] Cows and goats have been engineered to express drugs and other proteins in their milk, and in 2009 the FDA approved a drug produced in goat milk.[137][138] Other applications Genetic engineering has potential applications in conservation and natural area management. Gene transfer through viral vectors has been proposed as a means of controlling invasive species as well as vaccinating threatened fauna from disease.[139] Transgenic trees have been suggested as a way to confer resistance to pathogens in wild populations.[140] With the increasing risks of maladaptation in organisms as a result of climate change and other perturbations, facilitated adaptation through gene tweaking could be one solution to reducing extinction risks.[141] Applications of genetic engineering in conservation are thus far mostly theoretical and have yet to be put into practice. Genetic engineering is also being used to create microbial art.[142] Some bacteria have been genetically engineered to create black and white photographs.[143] Novelty items such as lavender-colored carnations,[144] blue roses,[145] and glowing fish[146][147] have also been produced through genetic engineering. Regulation Main article: Regulation of genetic engineering The regulation of genetic engineering concerns the approaches taken by governments to assess and manage the risks associated with the development and release of GMOs. The development of a regulatory framework began in 1975, at Asilomar, California.[148] The Asilomar meeting recommended a set of voluntary guidelines regarding the use of recombinant technology.[30] As the technology improved the US established a committee at the Office of Science and Technology,[149] which assigned regulatory approval of GM food to the USDA, FDA and EPA.[150] The Cartagena Protocol on Biosafety, an international treaty that governs the transfer, handling, and use of GMOs,[151] was adopted on 29 January 2000.[152] One hundred and fifty-seven countries are members of the Protocol, and many use it as a reference point for their own regulations.[153] The legal and regulatory status of GM foods varies by country, with some nations banning or restricting them, and others permitting them with widely differing degrees of regulation.[154][155][156][157] Some countries allow the import of GM food with authorisation, but either do not allow its cultivation (Russia, Norway, Israel) or have provisions for cultivation even though no GM products are yet produced (Japan, South Korea). Most countries that do not allow GMO cultivation do permit research.[158] Some of the most marked differences occur between the US and Europe. The US policy focuses on the product (not the process), only looks at verifiable scientific risks and uses the concept of substantial equivalence.[159] The European Union by contrast has possibly the most stringent GMO regulations in the world.[160] All GMOs, along with irradiated food, are considered "new food" and subject to extensive, case-by-case, science-based food evaluation by the European Food Safety Authority. The criteria for authorisation fall in four broad categories: "safety", "freedom of choice", "labelling", and "traceability".[161] The level of regulation in other countries that cultivate GMOs lie in between Europe and the United States. Regulatory agencies by geographical region Region Regulators Notes US USDA, FDA and EPA[150] Europe European Food Safety Authority[161] Canada Health Canada and the Canadian Food Inspection Agency[162][163] Regulated products with novel features regardless of method of origin[164][165] Africa Common Market for Eastern and Southern Africa[166] Final decision lies with each individual country.[166] China Office of Agricultural Genetic Engineering Biosafety Administration[167] India Institutional Biosafety Committee, Review Committee on Genetic Manipulation and Genetic Engineering Approval Committee[168] Argentina National Agricultural Biotechnology Advisory Committee (environmental impact), the National Service of Health and Agrifood Quality (food safety) and the National Agribusiness Direction (effect on trade)[169] Final decision made by the Secretariat of Agriculture, Livestock, Fishery and Food.[169] Brazil National Biosafety Technical Commission (environmental and food safety) and the Council of Ministers (commercial and economical issues)[169] Australia Office of the Gene Technology Regulator (oversees all GM products), Therapeutic Goods Administration (GM medicines) and Food Standards Australia New Zealand (GM food).[170][171] The individual state governments can then assess the impact of release on markets and trade and apply further legislation to control approved genetically modified products.[171] One of the key issues concerning regulators is whether GM products should be labeled. The European Commission says that mandatory labeling and traceability are needed to allow for informed choice, avoid potential false advertising[172] and facilitate the withdrawal of products if adverse effects on health or the environment are discovered.[173] The American Medical Association[174] and the American Association for the Advancement of Science[175] say that absent scientific evidence of harm even voluntary labeling is misleading and will falsely alarm consumers. Labeling of GMO products in the marketplace is required in 64 countries.[176] Labeling can be mandatory up to a threshold GM content level (which varies between countries) or voluntary. In Canada and the US labeling of GM food is voluntary,[177] while in Europe all food (including processed food) or feed which contains greater than 0.9% of approved GMOs must be labelled.[160] Controversy Main article: Genetically modified food controversies Critics have objected to the use of genetic engineering on several grounds, including ethical, ecological and economic concerns. Many of these concerns involve GM crops and whether food produced from them is safe and what impact growing them will have on the environment. These controversies have led to litigation, international trade disputes, and protests, and to restrictive regulation of commercial products in some countries.[178] Accusations that scientists are "playing God" and other religious issues have been ascribed to the technology from the beginning.[179] Other ethical issues raised include the patenting of life,[180] the use of intellectual property rights,[181] the level of labeling on products,[182][183] control of the food supply[184] and the objectivity of the regulatory process.[185] Although doubts have been raised,[186] economically most studies have found growing GM crops to be beneficial to farmers.[187][188][189] Gene flow between GM crops and compatible plants, along with increased use of selective herbicides, can increase the risk of "superweeds" developing.[190] Other environmental concerns involve potential impacts on non-target organisms, including soil microbes,[191] and an increase in secondary and resistant insect pests.[192][193] Many of the environmental impacts regarding GM crops may take many years to be understood and are also evident in conventional agriculture practices.[191][194] With the commercialisation of genetically modified fish there are concerns over what the environmental consequences will be if they escape.[195] There are three main concerns over the safety of genetically modified food: whether they may provoke an allergic reaction; whether the genes could transfer from the food into human cells; and whether the genes not approved for human consumption could outcross to other crops.[196] There is a scientific consensus[197][198][199][200] that currently available food derived from GM crops poses no greater risk to human health than conventional food,[201][202][203][204][205] but that each GM food needs to be tested on a case-by-case basis before introduction.[206][207][208] Nonetheless, members of the public are less likely than scientists to perceive GM foods as safe.[209][210][211][212] In popular culture Main article: Genetics in fiction § Genetic engineering Genetic engineering features in many science fiction stories.[213] Frank Herbert's novel The White Plague describes the deliberate use of genetic engineering to create a pathogen which specifically kills women.[213] Another of Herbert's creations, the Dune series of novels, uses genetic engineering to create the powerful Tleilaxu.[214] Few films have informed audiences about genetic engineering, with the exception of the 1978 The Boys from Brazil and the 1993 Jurassic Park, both of which make use of a lesson, a demonstration, and a clip of scientific film.[215][216] Genetic engineering methods are weakly represented in film; Michael Clark, writing for the Wellcome Trust, calls the portrayal of genetic engineering and biotechnology "seriously distorted"[216] in films such as The 6th Day. In Clark's view, the biotechnology is typically "given fantastic but visually arresting forms" while the science is either relegated to the background or fictionalised to suit a young audience.[216] In the 2007 video game, BioShock, genetic engineering plays an important role in the central storyline and universe. The game takes place in the fictional underwater dystopia Rapture, in which its inhabitants possess genetic superhuman abilities after injecting themselves with “plasmids”, a serum which grants such powers. Also in the city of Rapture are “Little Sisters”, little girls who are generically engineered, as well as a side-plot in which a cabaret singer sells her foetus to genetic scientists who implant false memories into the newborn and genetically engineer it to grow into an adult. See also Biological engineering Modifications (genetics) RNA editing#Therapeutic mRNA Editing Mutagenesis (molecular biology technique) The Nobel Prize in Physiology or Medicine (Swedish: Nobelpriset i fysiologi eller medicin) is awarded yearly by the Nobel Assembly at the Karolinska Institute for outstanding discoveries in physiology or medicine. The Nobel Prize is not a single prize, but five separate prizes that, according to Alfred Nobel's 1895 will, are awarded "to those who, during the preceding year, have conferred the greatest benefit to humankind". Nobel Prizes are awarded in the fields of Physics, Chemistry, Physiology or Medicine, Literature, and Peace. The Nobel Prize is presented annually on the anniversary of Alfred Nobel's death, 10 December. As of 2022, 114 Nobel Prizes in Physiology or Medicine have been awarded to 226 laureates, 214 men and 12 women. The first one was awarded in 1901 to the German physiologist, Emil von Behring, for his work on serum therapy and the development of a vaccine against diphtheria. The first woman to receive the Nobel Prize in Physiology or Medicine, Gerty Cori, received it in 1947 for her role in elucidating the metabolism of glucose, important in many aspects of medicine, including treatment of diabetes. The most recent Nobel prize was announced by the Karolinska Institute on 3 October 2022, and has been awarded to Swedish Svante Pääbo, for the discoveries concerning the genomes of extinct hominins and human evolution.[2] The prize consists of a medal along with a diploma and a certificate for the monetary award. The front side of the medal displays the same profile of Alfred Nobel depicted on the medals for Physics, Chemistry, and Literature; the reverse side is unique to this medal. Some awards have been controversial. This includes one to António Egas Moniz in 1949 for the prefrontal lobotomy, bestowed despite protests from the medical establishment. Other controversies resulted from disagreements over who was included in the award. The 1952 prize to Selman Waksman was litigated in court, and half the patent rights were awarded to his co-discoverer Albert Schatz who was not recognised by the prize. Nobel prizes cannot be awarded posthumously. Also, no more than three recipients can receive a Nobel Prize in Physiology or Medicine, a limitation that is sometimes discussed as an increasing trend for larger teams to conduct important scientific projects. Background Nobel was interested in experimental physiology and set up his own laboratories. Alfred Nobel was born on 21 October 1833 in Stockholm, Sweden, into a family of engineers.[3] He was a chemist, engineer and inventor who amassed a fortune during his lifetime, most of it from his 355 inventions, of which dynamite is the most famous.[4] He was interested in experimental physiology and set up his own labs in France and Italy to conduct experiments in blood transfusions. Keeping abreast of scientific findings, he was generous in his donations to Ivan Pavlov's laboratory in Russia and was optimistic about the progress resulting from scientific discoveries made in laboratories.[5] In 1888, Nobel was surprised to read his own obituary, titled "The merchant of death is dead", in a French newspaper. As it happened, it was Nobel's brother Ludvig who had died, but Nobel, unhappy with the content of the obituary and concerned that his legacy would reflect poorly on him, was inspired to change his will.[6] In his last will, Nobel requested that his money be used to create a series of prizes for those who confer the "greatest benefit on mankind" in physics, chemistry, peace, physiology or medicine, and literature.[7] Though Nobel wrote several wills during his lifetime, the last was written a little over a year before he died at the age of 63.[8] Because his will was contested, it was not approved by the Storting (Norwegian Parliament) until 26 April 1897.[9] After Nobel's death, the Nobel Foundation was set up to manage the assets of the bequest.[10] In 1900, the Nobel Foundation's newly created statutes were promulgated by Swedish King Oscar II.[11][12] According to Nobel's will, the Karolinska Institute in Sweden, a medical school and research centre, is responsible for the Prize in Physiology or Medicine.[13] Today, the prize is commonly referred to as the Nobel Prize in Medicine.[14] Nomination and selection The reverse side of the Nobel Prize for Physiology or Medicine It was important to Nobel that the prize be awarded for a "discovery" and that it be of "greatest benefit on mankind".[15] Per the provisions of the will, only select persons are eligible to nominate individuals for the award. These include members of academies around the world, professors of medicine in Sweden, Denmark, Norway, Iceland, and Finland, as well as professors of selected universities and research institutions in other countries. Past Nobel laureates may also nominate.[16] Until 1977, all professors of Karolinska Institute together decided on the Nobel Prize in Physiology or Medicine. That year, changes in Swedish law forced the institute to make public any documents pertaining to the Nobel Prize, and it was considered necessary to establish a legally independent body for the Prize work. Therefore, the Nobel Assembly was constituted, consisting of 50 professors at Karolinska Institute. It elects the Nobel Committee with five members who evaluate the nominees, the Secretary who is in charge of the organisation, and each year ten adjunct members to assist in the evaluation of candidates. In 1968, a provision was added that no more than three persons may share a Nobel prize.[17] True to its mandate, the committee has chosen researchers working in the basic sciences over those who have made applied science contributions. Harvey Cushing, a pioneering American neurosurgeon who identified Cushing's syndrome, was not awarded the prize, nor was Sigmund Freud, as his psychoanalysis lacks hypotheses that can be experimentally confirmed.[18] The public expected Jonas Salk or Albert Sabin to receive the prize for their development of the polio vaccines, but instead the award went to John Enders, Thomas Weller, and Frederick Robbins whose basic discovery that the polio virus could reproduce in monkey cells in laboratory preparations made the vaccines possible.[19] Through the 1930s, there were frequent prize laureates in classical physiology, but after that, the field began fragmenting into specialities. The last classical physiology laureates were John Eccles, Alan Hodgkin, and Andrew Huxley in 1963 for their findings regarding "unitary electrical events in the central and peripheral nervous system."[20] Prizes A Medicine or Physiology Nobel Prize laureate earns a gold medal, a diploma bearing a citation, and a sum of money.[21] These are awarded during the prize ceremony at the Stockholm Concert Hall. Medals Main article: Nobel Prize medal § Physiology and Medicine Alexander Fleming's 1945 Nobel Prize medal for Physiology and Medicine on display at the National Museum of Scotland, Edinburgh. The Physiology and Medicine medal has a portrait of Alfred Nobel in left profile on the obverse.[22] The medal was designed by Erik Lindberg.[22] The reverse of the medal depicts the 'Genius of Medicine holding an open book in her lap, collecting the water pouring out from a rock in order to quench a sick girl's thirst'.[23] It is inscribed "Inventas vitam iuvat excoluisse per artes" ("It is beneficial to have improved (human) life through discovered arts") an adaptation of "inventas aut qui vitam excoluere per artes" from line 663 from book 6 of the Aeneid by the Roman poet Virgil.[23] A plate below the figures is inscribed with the name of the recipient. The text "REG. UNIVERSITAS MED. CHIR. CAROL." denoting the Karolinska Institute is also inscribed on the reverse.[23] Between 1902 and 2010 the Nobel Prize medals were struck by the Myntverket, the Swedish royal mint, located in Eskilstuna. In 2011 the medals were made by the Det Norske Myntverket in Kongsberg. The medals have been made by Svenska Medalj in Eskilstuna since 2012.[22] Diplomas Nobel laureates receive a diploma directly from the King of Sweden. Each diploma is uniquely designed by the prize-awarding institutions for the laureate that receives it. In the case of the Nobel Prize in Physiology or Medicine, that is the Nobel Assembly at Karolinska Institute. Well-known artists and calligraphers from Sweden are commissioned to create it.[24] The diploma contains a picture and text which states the name of the laureate and a citation as to why they received the prize.[24] Award money At the awards ceremony, the laureate is given a document indicating the award sum. The amount of the cash award may differ from year to year, based on the funding available from the Nobel Foundation. For example, in 2009 the total cash awarded was 10 million SEK (US$1.4 million),[25] but in 2012, the amount was 8 million Swedish Krona, or US$1.1 million.[26] If there are two laureates in a particular category, the award grant is divided equally between the recipients, but if there are three, the awarding committee may opt to divide the grant equally, or award half to one recipient and a quarter to each of the two others.[27][28][29][30] Ceremony and banquet The awards are bestowed at a gala ceremony followed by a banquet.[31] The Nobel Banquet is an extravagant affair with the menu, planned months ahead of time, kept secret until the day of the event. The Nobel Foundation chooses the menu after tasting and testing selections submitted by selected chefs of international repute. Currently, it is a three-course dinner, although it was originally six courses in 1901. Each Nobel Prize laureate may bring up to 16 guests. Sweden's royal family attends, and typically the Prime Minister and other members of the government attend as well as representatives of the Nobel family.[32] Laureates For a more comprehensive list, see List of Nobel laureates in Physiology or Medicine. Nikolaas Tinbergen (left) and Konrad Lorenz (right) were awarded (with Karl von Frisch) for their discoveries concerning animal behaviour.[33] The first Nobel Prize in Physiology or Medicine was awarded in 1901 to the German physiologist Emil Adolf von Behring.[34] Behring's discovery of serum therapy in the development of the diphtheria and tetanus vaccines put "in the hands of the physician a victorious weapon against illness and deaths".[35][36] In 1902, the award went to Ronald Ross for his work on malaria, "by which he has shown how it enters the organism and thereby has laid the foundation for successful research on this disease and methods of combating it".[37] He identified the mosquito as the transmitter of malaria, and worked tirelessly on measures to prevent malaria worldwide.[38][39] The 1903 prize was awarded to Niels Ryberg Finsen, the first Faroese laureate, "in recognition of his contribution to the treatment of diseases, especially lupus vulgaris, with concentrated light radiation, whereby he has opened a new avenue for medical science".[40][41] He died within a year after receiving the prize at the age of 43.[42] Ivan Pavlov, whose work Nobel admired and supported, received the prize in 1904 for his work on the physiology of digestion.[43] Subsequently, those selecting the recipients have exercised wide latitude in determining what falls under the umbrella of Physiology or Medicine. The awarding of the prize in 1973 to Nikolaas Tinbergen, Konrad Lorenz, and Karl von Frisch for their observations of animal behavioural patterns could be considered a prize in the behavioural sciences rather than medicine or physiology.[14] Tinbergen expressed surprise in his Nobel Prize acceptance speech at "the unconventional decision of the Nobel Foundation to award this year's prize 'for Physiology or Medicine' to three men who had until recently been regarded as 'mere animal watchers'".[44] In 1947, Gerty Cori was the first woman to be awarded the Prize in Physiology or Medicine. Laureates have been awarded the Nobel Prize in a wide range of fields that relate to physiology or medicine. As of 2010, eight Prizes have been awarded for contributions in the field of signal transduction through G proteins and second messengers. 13 have been awarded for contributions in the field of neurobiology[45] and 13 have been awarded for contributions in Intermediary metabolism.[46] The 100 Nobel Prizes in Physiology or Medicine have been awarded to 195 individuals through 2009.[47][48] Twelve women have received the prize: Gerty Cori (1947), Rosalyn Yalow (1977), Barbara McClintock (1983), Rita Levi-Montalcini (1986), Gertrude B. Elion (1988), Christiane Nüsslein-Volhard (1995), Linda B. Buck (2004), Françoise Barré-Sinoussi (2008), Elizabeth H. Blackburn (2009), Carol W. Greider (2009), May-Britt Moser (2014) and Youyou Tu (2015).[49] Only one woman, Barbara McClintock, has received an unshared prize in this category, for the discovery of genetic transposition.[47][50] Mario Capecchi, Martin Evans, and Oliver Smithies were awarded the prize in 2007 for the discovery of a gene targeting procedure (a type of genetic recombination) for introducing homologous recombination in mice, employing embryonic stem cells through the development of the knockout mouse.[51][52] There have been 38 times when the Nobel Prize in Physiology or Medicine was awarded to a single individual, 31 times when it was shared by two, and 33 times there were three laureates (the maximum allowed). In 2009, the Nobel Prize was awarded to Elizabeth Blackburn, Carol W. Greider and Jack W. Szostak of the United States for discovering the process by which chromosomes are protected by telomeres (regions of repetitive DNA at the ends of chromosomes) and the enzyme telomerase; they shared the prize of 10,000,000 SEK (slightly more than €1 million, or US$1.4 million).[53] Rita Levi-Montalcini, an Italian neurologist, who together with colleague Stanley Cohen, received the 1986 Nobel Prize in Physiology or Medicine for their discovery of Nerve growth factor (NGF), was the first Nobel laureate to reach the 100th birthday.[48] Time factor and death Ralph M. Steinman was an inadvertent posthumous recipient of the Prize. Because of the length of time that may pass before the significance of a discovery becomes apparent, some prizes are awarded many years after the initial discovery. Barbara McClintock made her discoveries in 1944, before the structure of the DNA molecule was known; she was not awarded the prize until 1983. Similarly, in 1916 Peyton Rous discovered the role of tumor viruses in chickens, but was not awarded the prize until 50 years later, in 1966.[54] Nobel laureate Carol Greider's research leading to the prize was conducted over 20 years before. She noted that the passage of time is an advantage in the medical sciences, as it may take many years for the significance of a discovery to become apparent.[55] In 2011, Canadian immunologist Ralph M. Steinman was awarded the prize; however, unbeknownst to the committee, he had died three days before the announcement. The committee decided that since the prize was awarded "in good faith," it would be allowed to stand. Controversial inclusions and exclusions Main article: Nobel Prize controversies Some of the awards have been controversial. The person who was deserving of the 1923 prize for the discovery of insulin as a central hormone for controlling diabetes (awarded only a year after its discovery)[56] has been heatedly debated. It was shared between Frederick Banting and John Macleod; this infuriated Banting who regarded Macleod's involvement as minimal. Macleod was the department head at the University of Toronto but otherwise was not directly involved in the findings. Banting thought his laboratory partner Charles Best, who had shared in the laboratory work of discovery, should have shared the prize with him as well. In fairness, he decided to give half of his prize money to Best. Macleod on his part felt the biochemist James Collip, who joined the laboratory team later, deserved to be included in the award and shared his prize money with him.[56] Some maintain that Nicolae Paulescu, a Romanian professor of physiology at the University of Medicine and Pharmacy in Bucharest, was the first to isolate insulin, in 1916, although his pancrein was an impure aqueous extract unfit for human treatment similar to the one used previously by Israel Kleiner.[57][58][59] When Banting published the paper that brought him the Nobel,[60] Paulescu already held a patent for his discovery (10 April 1922, patent no. 6254 (8322) "Pancreina şi procedeul fabricaţiei ei"/"Pancrein and the process of making it", from the Romanian Ministry of Industry and Trade).[61][62][63] The Spanish neurophysiologist Fernando de Castro (1896–1967) was the first to describe arterial chemoreceptors and circumscribe them to the carotid body for the respiratory reflexes in 1926–1928. For many experts, this direct disciple of Santiago Ramón y Cajal deserved to share the Nobel Prize 1938 with the awarded Corneille Heymans, but at that time Spain was immersed in the Spanish Civil War and it seems that the Nobel Board even doubted if he was alive or not, being at the front since almost the beginning of the conflict. Heymans himself recognised the merits of De Castro for the Nobel Prize in different occasions, including a famous talk in Montevideo (Uruguay).[64] Scandal and controversy resulted from the 2008 award to Harald zur Hausen for the discovery of HPV, and to Françoise Barré-Sinoussi and Luc Montagnier for discovering HIV. In 1949, despite protests from the medical establishment, the Portuguese neurologist António Egas Moniz received the Physiology or Medicine Prize for his development of the prefrontal leucotomy, which he promoted by declaring the procedure's success just 10 days postoperative. Due largely to the publicity surrounding the award, it was prescribed without regard for modern medical ethics. Favourable results were reported by such publications as The New York Times. It is estimated that around 40,000 lobotomies were performed in the United States before the procedure's popularity faded.[65] Rosemary Kennedy, the sister of John F. Kennedy, was subjected to the procedure by their father; it incapacitated her to the extent that she needed to be institutionalised for the rest of her life.[66][67] The 1952 prize, awarded solely to Selman Waksman for his discovery of streptomycin, omitted the recognition some felt due to his co-discoverer Albert Schatz.[68][69] There was litigation brought by Schatz against Waksman over the details and credit of the streptomycin discovery; Schatz was awarded a substantial settlement, and, together with Waksman, Schatz was to be officially recognised as a co-discoverer of streptomycin as concerned patent rights. He is not a Nobel Prize laureate.[68] The 1962 Prize awarded to James D. Watson, Francis Crick, and Maurice Wilkins—for their work on DNA structure and properties—did not recognise contributing work from others, such as Alec Stokes and Herbert Wilson. In addition, Erwin Chargaff, Oswald Avery, and Rosalind Franklin (whose key DNA x-ray crystallography work was the most detailed yet least acknowledged among the three)[70][page needed] contributed directly to the ability of Watson and Crick to solve the structure of the DNA molecule. Avery died in 1955, Franklin died in 1958 and posthumous nominations for the Nobel Prize are not permitted. Files of Nobel Prize nominations show Franklin was not nominated when she was alive.[71] As a result of Watson's misrepresentations of Franklin and her role in the discovery of the double helix in his book The Double Helix, Franklin has come to be portrayed as a classic victim of sexism in science.[72][73] Chargaff, for his part, was not quiet about his exclusion from the prize, bitterly writing to other scientists about his disillusionment regarding the field of molecular biology.[74] The 2008 award went to Harald zur Hausen in recognition of his discovery that human papillomavirus (HPV) can cause cervical cancer, and to Françoise Barré-Sinoussi and Luc Montagnier for discovering the human immunodeficiency virus (HIV).[75] Whether Robert Gallo or Luc Montagnier deserved more credit for the discovery of the virus that causes AIDS has been a matter of considerable controversy. As it was, Gallo was left out and not awarded a prize.[76][77] Additionally, there was a scandal when it was learned that Harald zur Hausen was being investigated for having a financial interest in vaccines for the cervical cancer that HPV can cause. AstraZeneca, which with a stake in two lucrative HPV vaccines could benefit financially from the prize, had agreed to sponsor Nobel Media and Nobel Web. According to Times Online, two senior figures in the selection process that chose zur Hausen also had strong links with AstraZeneca.[78] Limits on number of awardees The provision that restricts the maximum number of nominees to three for any one prize, introduced in 1968, has caused considerable controversy.[17][79] From the 1950s onward, there has been an increasing trend to award the Nobel Prize in Physiology or Medicine to more than one person. There were 59 people who received the prize in the first 50 years of the last century, while 113 individuals received it between 1951 and 2000. This increase could be attributed to the rise of the international scientific community after World War II, resulting in more persons being responsible for the discovery, and nominated for, a particular prize. Also, current biomedical research is more often carried out by teams rather than by scientists working alone, making it unlikely that any one scientist, or even a few, is primarily responsible for a discovery;[19] this has meant that a prize nomination that would have to include more than three contributors is automatically excluded from consideration.[54] Also, deserving contributors may not be nominated at all because the restriction results in a cut-off point of three nominees per prize, leading to controversial exclusions.[15] Years without awards There have been nine years in which the Nobel Prize in Physiology or Medicine was not awarded (1915–1918, 1921, 1925, 1940–1942). Most of these occurred during either World War I (1914–1918) or World War II (1939–1945).[48] In 1939, Nazi Germany for English biochemist Richard John Roberts shared the 1993 Nobel Prize in physiology or medicine with American biochemist Phillip Allen Sharp (1944-) for their independent discovery of split genes. Roberts worked at the Cold Spring Harbor Laboratory in New York, and Sharp did his research at the Massachusetts Institute of Technology (MIT) in Cambridge, Mass. Each announced his research results in 1977. Their discovery transformed the model for understanding how proteins are synthesized from genes. The discovery of split genes led to the prediction of a new genetic process, gene splicing, which is essential for expressing genetic information. Richard J. Roberts was born on September 6, 1943, in Derby, England. He was awarded the BS degree from the University of Sheffield in 1965. He remained at the university for postgraduate work and earned a PhD degree in organic chemistry in 1968. In 1969, Roberts left England for training in the United States. He became a research fellow at Harvard University in Cambridge, Mass, where he worked until 1972. In 1972, he became a senior staff investigator at the Cold Spring Harbor Laboratory in southeastern New York, and in 1987, he became assistant director of the laboratory. He left the laboratory in 1992 to become research director of eukaryotic (nucleated cells) research at New England Biolab, a biotechnology firm in Beverly, Mass. Roberts did his Nobel Prize-winning research on the adenovirus, the virus that causes the common cold, at the Cold Spring Harbor Laboratory. In 1977, Roberts and his team of Thomas Broker, Louise Chow, and Richard Gelinas established that the genes of the adenovirus are discontinuous: the segments of DNA that code for protein are interrupted by lengthy stretches of DNA that do not contain genetic information. The coding segments are called exons and the noncoding ones, introns. Also in 1977, a research team supervised by Sharp at MIT made the same discovery that Roberts did. Previously, on the basis of studies of bacterial DNA, biologists believed that genes consisted of unbroken stretches of DNA, all of which encoded protein structure. Since the discovery by Roberts and Sharp, it has been established that the discontinuous gene structure is the most frequent structure found in higher organisms, including humans. In addition to having important implications for the study of genetic diseases, this structure is believed to drive evolution by allowing information from different parts of the gene to be brought together in new combinations. The general view is that evolution occurs through the accumulation of mutations or minor alterations in the genetic material that produces a gradual change in the overall organism. However, gene splitting suggests that another mechanism may be important in the evolution of higher organisms—the rearrangement of genetic information into new protein-coding units to speed up evolution and to respond more flexibly to environmental challenges. Errors in gene splicing are known to be the basis of several disorders, including β-thalassemia (a form of anemia) and chronic myelogenous leukemia. Besides the Nobel Prize, Roberts has received many awards and honors. He was elected a fellow of the Royal Society of London in 1979, and in 2000, he was honored on a stamp issued by the Palau Islands. was born in 1943, the only child of John and Edna Roberts (née Allsop) in Derby, England. My father was a motor mechanic and my mother a homemaker. We moved to Bath when I was four and so I consider myself a Bathonian. My elementary education was at Christ Church infant school and St. Stephen’s junior school. At St. Stephen’s I encountered my first real mentor, the headmaster Mr. Broakes. He must have spotted something unusual in me for he spent lots of time encouraging my interest in mathematics. He would produce problems and puzzles for me to solve and I still enjoy the challenge of crossword and logical puzzles. Most importantly, I learned that logic and mathematics are fun! After passing the “dreaded” 11 + exam I moved on to the City of Bath Boys (now Beechen Cliff) School. At this time I wanted to be a detective, where it seemed they paid you to solve puzzles. This changed quickly when I received a chemistry set as a present. I soon exhausted the experiments that came with the set and started reading about less mundane ones. More interesting apparatus like Bunsen burners, retorts, flasks and beakers were purchased. My father, ever supportive of my endeavors, arranged for the construction of a large chemistry cabinet complete with a formica top, drawers, cupboards and shelves. This was to be my pride and joy for many years. Through my father, I met a local pharmacist who became a source of chemicals that were not in the toy stores. I soon discovered fireworks and other concoctions. Luckily, I survived those years with no serious injuries or burns. I knew I had to be a chemist. I am a passionate reader, having been tutored very early by my mother. I avidly devoured all books on chemistry that I could find. Formal chemistry at school seemed boring by comparison and my performance was routine. In contrast, I did spectacularly well in mathematics and sailed through classes and exams with ease. During these years at school I also discovered chess, which I loved, and billiards and snooker, which became a consuming passion. At age 15, I easily passed the O-level examinations and then began to specialize in the sciences taking Mathematics, Physics and Chemistry. For exercise I discovered the sport of caving and would spend most weekends underground on the nearby Mendips. From age 16 on I found school boring and failed A-level Physics at my first attempt. This was necessary for University entrance and so I stayed an extra year to repeat it. This time I did splendidly and was admitted to Sheffield University, my first choice because of their excellent Chemistry Department. After Chemistry, Physics and Mathematics in the first year, I opted for Biochemistry as a subsidiary subject in the second year. I loathed it. The lectures merely required rote learning and the laboratory consisted of the most dull experiments imaginable. I was grateful when that year was over and could concentrate wholly on Chemistry. I graduated in 1965 with an upper second class honours degree. As an undergraduate, David Ollis, the Professor of Organic Chemistry, really caught my imagination. His course emphasized problem solving, not memorization – more puzzles! Fortunately, he accepted me as his Ph.D. student and I began to explore the neoflavonoids found in a piece of heartwood from a Brazilian tree. Two pieces of luck followed. My tree contained more than its fair share of interesting new compounds and I was put in a lab with an exceptional postdoctoral fellow, Kazu Kurosawa, who proved a gifted teacher. Not only did he suggest the right experiments he explained why they should be done. Within one year I had essentially enough for my thesis and an understanding of how to do research. I had the luxury of spending the next two years following my nose, reading and experimenting. During this time I came across a book, by John Kendrew, that was to change the course of my research career. It described the early history of crystallography and molecular biology focussing on the MRC Laboratory in Cambridge. It was my first exposure to “molecular biology” and I became hooked. For postdoctoral studies, I looked for a laboratory doing biochemistry that might accept an organic chemist and provide a pathway into molecular biology. Luckily, Jack Strominger offered me a position, not in Wisconsin as I had thought, but at Harvard where he had just been appointed Professor of Biochemistry and Molecular Biology. It was on January 1st, 1969, that my family walked across the runway at Logan Airport with an outside temperature of 4°F and a massive wind blowing, to start a new life. The next four years were wonderful. Mostly, I learned, although at first I was in a fog. Everyone spoke in acronyms: DNA, RNA, ATP, UDP, GlcNAc. Luckily two Australians, Aubrey Egan and Allen Warth, lived close to my apartment and we would drive in and out of the lab together each day. Those half hour commutes became my biochemistry classroom. Slowly I learned the jargon. A third Australian, Tom Stewart patiently guided me into the world of tRNAs since it was his project that I was to pick up. I was assigned the job of sequencing a tRNA that was involved in bacterial cell wall biosynthesis. In 1969, only a handful of tRNAs had been sequenced previously, mostly by chemical techniques introduced by Holly and his contemporaries. However, within a few months and much reading, I decided that a new method, being pioneered in Fred Sanger‘s lab in Cambridge, was much better. In late 1970, I had succeeded in making enough pure tRNAGly to start sequencing and set off for a one month sojourn in Cambridge to learn the techniques. What a wonderful time! I don’t remember sleeping, but I do remember the excitement of meeting Fred and the other famous researchers, many of whom had featured in Kendrew’s book. This was a heady experience that validated my decision to be a molecular biologist. On my return to Harvard, my small sequencing operation was the first in the Boston area and many researchers came to learn the techniques. My own sequencing was successful and I managed two Nature papers during this postdoctoral period. When it came time to leave Harvard I wanted to return to the UK and applied for a job in Edinburgh. In the meantime, I was approached by Mark Ptashne, who told me that Jim Watson (“the” Watson) was looking for someone to sequence SV40. I had not met Jim previously and I was over-awed when he offered me the job after a 10 minute meeting, during which I mainly listened! It was a challenging project made all the more exciting by Jim’s description and his offer of a good salary, money to support a lab and all necessary set-up money. With a month to decide and no word from Edinburgh, I decided the offer was too good to turn down. In September, 1972, I moved to Cold Spring Harbor. Earlier in 1972, I attended a seminar at Harvard Medical School given by Dan Nathans. He described an enzyme, Endonuclease R, that could cleave DNA into specific pieces. This was to shape much of my subsequent research career. Sanger had developed RNA sequencing because there were plenty of small RNA molecules to practice on, but no suitable DNA molecules. I realized that Nathans’ restriction enzyme gave an immediate way to isolate small DNA molecules. Surely there must be more restriction enzymes with different specificities. DNA sequencing seemed within reach and I was exhilarated. Upon moving to Cold Spring Harbor, I set out to make preparations of Endonuclease R and the few other restriction enzymes known at the time. We also began a systematic search for new ones. I also made some DNA, since I had never worked with it before! A key factor in our restriction enzyme success was a highly talented technician, Phyllis Myers, who joined me in 1973. She became the keeper of our enzyme collection and a valuable resource to scientists around the world. We constantly sent samples to other researchers and were inundated with visitors. Every meeting at Cold Spring Harbor brought a few people carrying tubes of DNA to see if we had an enzyme that would cut it. Three quarters of the world’s first restriction enzymes were discovered or characterized in my laboratory. I made a lot of friends in those days! Plans to sequence SV40 DNA were abandoned shortly after reaching Cold Spring Harbor. Instead we turned our attention to Adenovirus-2 DNA. Ulf Pettersson had brought this system to the laboratory shortly before my arrival and it seemed a good model system because it was similar in size to bacteriophage lambda, where many spectacular advances in prokaryotic molecular biology had taken place. We began to map the DNA. Similar work was being carried out in Joe Sambrook’s lab at Cold Spring Harbor and eventually led to the only joint publication I have with Phil Sharp. In 1974, Richard Gelinas, whom I had first met at Harvard, joined my laboratory to characterize the initiation and termination signals for an Adenovirus-2 mRNA. The idea was to sequence the 5′-end of an mRNA, map its location on a restriction fragment, and then sequence the upstream region. This would be the promoter. Shortly after beginning the project, mRNA caps were discovered and we developed an assay for capped oligonucleotides. All seemed well until we came up with the startling finding that all late mRNAs seemed to begin with the same capped oligonucleotide, which was not encoded on the DNA next to the main body of the mRNA. We had excellent biochemical evidence for this, but real proof was elusive. In March, 1977, I hit on the right experiment to show that our proposed split structure for Adenovirus-2 mRNAs was correct. Louise Chow and Tom Broker, two talented electron microscopists, agreed to collaborate with us on the crucial experiment. We hoped to visualize the split structure by hybridizing an intact mRNA to its two different coding regions. Based on a guess about the location of the coding region for the 5′-end, we made appropriate DNA fragments. The reason for our guess turned out to be wrong, but luckily the fragment worked anyway! Finally, by direct visualization we could see the split genes in the electron microscope. Our own work turned to an analysis of the sequences involved in RNA splicing. Joe Sambrook and Walter Keller cloned the common leader sequence at the 5′-end of late Adenovirus-2 mRNAs and Sayeeda Zain in my lab sequenced it. Later we undertook the complete sequence of Adenovirus-2 DNA. This required a lot of computer software development and I was fortunate to have Richard Gelinas and Tom Gingeras spearheading this effort. In 1978, this was still a relatively new activity and not considered particularly biological. I had trouble convincing Jim Watson that computers were essential for modern biology and for several years we operated remotely through Stony Brook University. Eventually, I managed to get funding from NIH (Phil Sharp was chairman of a site-visit team that reviewed this grant) and we are still active in this area. My most recent work has been in the area of DNA methylases as outlined in the Nobel Lecture. In 1992 I moved to New England Biolabs, a small private company of 150 individuals making research reagents, most notably restriction enzymes, and carrying out basic research. In 1974 I had tried unsuccessfully to convince Jim Watson that Cold Spring Harbor should start a company to manufacture and sell restriction enzymes. He declined, thinking there was no money to be made. Soon after this I met Don Comb, the president and founder of New England Biolabs, who had a small basement operation going with himself, his wife and one technician. They were about to start selling the first restriction enzyme. I told him about our rapidly growing collection and was appointed their chief consultant. I am now joint Research Director with my good friend, Ira Schildkraut. The main theme of my work in biology has centered on the belief that we must know the structure of the molecules we work with if we are to understand how they function. This means knowing the sequence of macromolecules and cataloguing any modifications such as methylation. For proteins, 3-dimensional structure and post-translational modification are crucial. This latter area is a target for my future work. Throughout my life in science I have been fortunate to have friends and family who will bring me back to earth and remind me that there is much in life to be savored besides Science. I enjoy music very much and love to collect and play games, especially video games. I am indebted to my wife Jean, and my children, Alison, Andrew, Christopher and Amanda who have been a source of great joy and comfort. George Andrew Olah (born Oláh András György; May 22, 1927 – March 8, 2017) was a Hungarian-American chemist. His research involved the generation and reactivity of carbocations via superacids. For this research, Olah was awarded a Nobel Prize in Chemistry in 1994 "for his contribution to carbocation chemistry."[3] He was also awarded the Priestley Medal, the highest honor granted by the American Chemical Society and F.A. Cotton Medal for Excellence in Chemical Research of the American Chemical Society in 1996.[4][5][6] After the Hungarian Revolution of 1956, he emigrated to the United Kingdom, which he left for Canada in 1964, finally resettling in the United States in 1965. According to György Marx, he was one of The Martians.[7] Early life and education Olah was born in Budapest, Hungary, on May 22, 1927, into a Jewish couple, Magda (Krasznai) and Gyula Oláh, a lawyer.[8][9] After the high school of Budapesti Piarist Gimnazium,[10] he studied under organic chemist Géza Zemplén at the Technical University of Budapest, now the Budapest University of Technology and Economics, where he earned M.S. and Ph.D degrees in chemical engineering.[11] From 1949 through 1954, he taught at the school as a professor of organic chemistry.[12] In the subsequent two years, from 1954 to 1956, he worked at the research institute of the Hungarian Academy of Sciences, where he was associate scientific director and head of the department of organic chemistry.[12] Career and research As a result of the 1956 Hungarian Revolution, he and his family moved briefly to England and then to Canada, where he joined Dow Chemical in Sarnia, Ontario, with another Hungarian chemist, Stephen J. Kuhn. Olah's pioneering work on carbocations started during his eight years with Dow.[13] In 1965, he returned to academia at Case Western Reserve University in Cleveland, Ohio, chairing the department of chemistry from 1965 to 1969, and from 1967 through 1977 he was the C. F. Maybery Distinguished Professor of Research in Chemistry.[12] In 1971, Olah became a naturalized citizen of the United States.[11] He then moved to the University of Southern California in 1977.[11] At USC, Olah was a distinguished professor and the director of the Loker Hydrocarbon Research Institute.[14] Starting in 1980, he served as the Distinguished Donald P. and Katherine B. Loker Professor of Chemistry and later became a distinguished professor in USC's school of engineering.[11] In 1994, Olah was awarded the Nobel Prize in Chemistry "for his contribution to carbocation chemistry".[15] In particular, Olah's search for stable nonclassical carbocations led to the discovery of protonated methane stabilized by superacids, like FSO3H-SbF5 ("Magic Acid"). CH4 + H+ → CH5+ Because these cations were able to be stabilized, scientists could now use infrared spectroscopy and nuclear magnetic resonance (NMR) spectroscopy to study them in greater depth, as well as use them as catalysts in organic synthesis reactions.[16] Olah, with Canadian chemist Saul Winstein, was also involved in a career-long battle with Herbert C. Brown of Purdue over the existence of so-called "nonclassical" carbocations – such as the norbornyl cation, which can be depicted as cationic character delocalized over several bonds.[17] Olah's studies of the cation with NMR spectroscopy provided more evidence suggesting that Winstein's model of the non-classical cation, "featuring a pair of [delocalized] electrons smeared between three carbon atoms," was correct.[18] In 1997, the Olah family formed an endowment fund (the George A. Olah Endowment) which grants annual awards to outstanding chemists, including the George A. Olah Award in Hydrocarbon or Petroleum Chemistry, formerly known as the ACS Award in Petroleum Chemistry. The awards are selected and administered by the American Chemical Society.[19] Later in his career, his research shifted from hydrocarbons and their transformation into fuel to the methanol economy, namely generating methanol from methane.[20] He joined with Robert Zubrin, Anne Korin, and James Woolsey in promoting a flexible-fuel mandate initiative.[21][22][23] In 2005, Olah wrote an essay promoting the methanol economy in which he suggested that methanol could be produced from hydrogen gas (H2) and industrially derived or atmospheric carbon dioxide (CO2), using energy from renewable sources to power the production process.[24] Personal life He married Judit Ágnes Lengyel (Judith Agnes Lengyel) in 1949, and they had two children, György (George), born in Hungary in 1954, and Ronald, born in the U.S. in 1959.[11] Olah died on March 8, 2017, at his home in Beverly Hills, California.[25][26] After his death, the Hungarian government said that the "country has lost a great patriot and one of the most outstanding figures of Hungarian scientific life."[25] Awards and honours Olah in 2010 1970 ACS Henry Morley Medal[12] 1989 California Scientist of the Year[12] 1989 Roger Adams Award in Organic Chemistry[12] 1993 Chemical Pioneer Award from the American Institute of Chemists[27] 1994 Nobel Prize in Chemistry[3] 1996 ACS F. A. Cotton Medal[28] 1996 Golden Plate Award of the American Academy of Achievement[29] 1997 Elected a Foreign Member of the Royal Society (ForMemRS) in 1997.[1] 2001 Arthur C. Cope Award 2001 Elected a member of the American Philosophical Society[30] 2005 Priestley Medal from the American Chemical Society The Nobel Prize in Chemistry (Swedish: Nobelpriset i kemi) 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 the Royal Swedish Academy of Sciences on proposal of the Nobel Committee for Chemistry which consists of five members elected by the Academy. The award is presented in Stockholm at an annual ceremony on 10 December, the anniversary of Nobel's death. The first Nobel Prize in Chemistry was awarded in 1901 to Jacobus Henricus van 't Hoff, of the Netherlands, "for his discovery of the laws of chemical dynamics and osmotic pressure in solutions". From 1901 to 2022, the award has been bestowed on a total of 189 individuals.[2] The 2022 Nobel Prize in Chemistry was awarded to Carolyn R. Bertozzi, Morten P. Meldal, and Karl Barry Sharpless for the development of click chemistry and bioorthogonal chemistry. As of 2022 only eight women had won the prize: Marie Curie, her daughter Irène Joliot-Curie, Dorothy Hodgkin (1964), Ada Yonath (2009), Frances Arnold (2018), Emmanuelle Charpentier and Jennifer Doudna (2020), and Carolyn R. Bertozzi (2022).[3] Background Alfred Nobel stipulated in his last will and testament that his money be used to create a series of prizes for those who confer the "greatest benefit on mankind" in physics, chemistry, peace, physiology or medicine, and literature.[4][5] Though Nobel wrote several wills during his lifetime, the last was written a little over a year before he died, and signed at the Swedish-Norwegian Club in Paris on 27 November 1895.[6][7] Nobel bequeathed 94% of his total assets, 31 million Swedish kronor (US$198 million, €176 million in 2016), to establish and endow the five Nobel Prizes.[8] Due to the level of skepticism surrounding the will, it was not until 26 April 1897 that it was approved by the Storting (Norwegian Parliament).[9][10] The executors of his will were Ragnar Sohlman and Rudolf Lilljequist, who formed the Nobel Foundation to take care of Nobel's fortune and organise the prizes. The members of the Norwegian Nobel Committee that were to award the Peace Prize were appointed shortly after the will was approved. The prize-awarding organisations followed: the Karolinska Institutet on 7 June, the Swedish Academy on 9 June, and the Royal Swedish Academy of Sciences on 11 June.[11][12] The Nobel Foundation then reached an agreement on guidelines for how the Nobel Prize should be awarded. In 1900, the Nobel Foundation's newly created statutes were promulgated by King Oscar II.[10][13][14] According to Nobel's will, The Royal Swedish Academy of Sciences were to award the Prize in Chemistry.[14] Award ceremony Main article: Nobel Prize The committee and institution serving as the selection board for the prize typically announce the names of the laureates in October. The prize is then awarded at formal ceremonies held annually on 10 December, the anniversary of Alfred Nobel's death. "The highlight of the Nobel Prize Award Ceremony in Stockholm is when each Nobel Laureate steps forward to receive the prize from the hands of His Majesty the King of Sweden. The Nobel Laureate receives three things: a diploma, a medal and a document confirming the prize amount" ("What the Nobel Laureates Receive"). Later the Nobel Banquet is held in Stockholm City Hall. A maximum of three laureates and two different works may be selected. The award can be given to a maximum of three recipients per year. It consists of a gold medal, a diploma, and a cash grant.[citation needed] Nomination and selection For a more comprehensive list, see List of nominees for the Nobel Prize in Chemistry. In 1901, Jacobus Henricus van 't Hoff (1852–1911) received the first Nobel Prize in Chemistry. The Nobel Laureates in chemistry are selected by a committee that consists of five members elected by the Royal Swedish Academy of Sciences. In its first stage, several thousand people are asked to nominate candidates. These names are scrutinized and discussed by experts until only the laureates remain. This slow and thorough process, is arguably what gives the prize its importance. Forms, which amount to a personal and exclusive invitation, are sent to about three thousand selected individuals to invite them to submit nominations. The names of the nominees are never publicly announced, and neither are they told that they have been considered for the Prize. Nomination records are sealed for fifty years. In practice, some nominees do become known. It is also common for publicists to make such a claim – founded or not. The nominations are screened by committee, and a list is produced of approximately two hundred preliminary candidates. This list is forwarded to selected experts in the field. They remove all but approximately fifteen names. The committee submits a report with recommendations to the appropriate institution. While posthumous nominations are not permitted, awards can occur if the individual died in the months between the nomination and the decision of the prize committee. The award in chemistry requires the significance of achievements being recognized is "tested by time". In practice it means that the lag between the discovery and the award is typically on the order of 20 years and can be much longer. As a downside of this approach, not all scientists live long enough for their work to be recognized. Some important scientific discoveries are never considered for a Prize, as the discoverers may have died by the time the impact of their work is realized. Prizes A Chemistry Nobel Prize laureate earns a gold medal, a diploma bearing a citation, and a sum of money.[15] Nobel Prize medals Main article: Nobel Prize medal § Physics and Chemistry The medal for the Nobel Prize in Chemistry is identical in design to the Nobel Prize in Physics medal.[16][17] The reverse of the physics and chemistry medals depict the Goddess of Nature in the form of Isis as she emerges from clouds holding a cornucopia. The Genius of Science holds the veil which covers Nature's 'cold and austere face'.[17] It was designed by Erik Lindberg and is manufactured by Svenska Medalj in Eskilstuna.[17] It is inscribed "Inventas vitam iuvat excoluisse per artes" ("It is beneficial to have improved (human) life through discovered arts") an adaptation of "inventas aut qui vitam excoluere per artes" from line 663 from book 6 of the Aeneid by the Roman poet Virgil.[18] A plate below the figures is inscribed with the name of the recipient. The text "REG. ACAD. SCIENT. SUEC." denoting the Royal Swedish Academy of Sciences is inscribed on the reverse.[17] Nobel Prize diplomas Nobel laureates receive a diploma directly from the hands of the King of Sweden. Each diploma is uniquely designed by the prize-awarding institutions for the laureate that receives it. The diploma contains a picture and text which states the name of the laureate and normally a citation of why they received the prize.[19] Award money At the awards ceremony, the laureate is given a document indicating the award sum. The amount of the cash award may differ from year to year, based on the funding available from the Nobel Foundation. For example, in 2009 the total cash awarded was 10 million SEK (US$1.4 million),[20] but in 2012, the amount was 8 million Swedish Krona, or US$1.1 million.[21] If there are two laureates in a particular category, the award grant is divided equally between the recipients, but if there are three, the awarding committee may opt to divide the grant equally, or award half to one recipient and a quarter to each of the two others.[22][23][24][25] Nobel laureates in chemistry by nationality For a more comprehensive list, see List of Nobel laureates in Chemistry. Country Laureates[A]  United States 79  Germany 34  United Kingdom  France 10  Japan 8  Switzerland 7  Israel 6  Canada 5  Sweden  Netherlands 4  Hungary 3  Austria 2  Denmark  New Zealand  Norway  Poland  Argentina 1  Australia  Belgium  Czech Republic  Egypt  Finland  India  Italy  Mexico  Romania  Russia  Turkey  Taiwan Scope of award In recent years, the Nobel Prize in Chemistry has drawn criticism from chemists who feel that the prize is more frequently awarded to non-chemists than to chemists.[26] In the 30 years leading up to 2012, the Nobel Prize in Chemistry was awarded ten times for work classified as biochemistry or molecular biology, and once to a materials scientist. In the ten years leading up to 2012, only four prizes were awarded for work strictly in chemistry.[26] Commenting on the scope of the award, The Economist explained that the Royal Swedish Academy of Sciences is bound by Nobel's bequest, which specifies awards only in physics, chemistry, literature, medicine, and peace. Biology was in its infancy in Nobel's day and no award was established. The Economist argued there is no Nobel Prize for mathematics either, another major discipline, and added that Nobel's stipulation of no more than three winners is not readily applicable to modern physics, where progress is typically made through huge collaborations rather than by individuals alone.[27] In 2020, Ioannidis et al. reported that half of the Nobel Prizes for science awarded between 1995–2017 were clustered in just a few disciplines within their broader fields. Atomic physics, particle physics, cell biology, and neuroscience dominated the two subjects outside chemistry, while molecular chemistry was the chief prize-winning discipline in its domain. Molecular chemists won 5.3% of all science Nobel Prizes during this period.[28] 4 George A. Olah - Facts The Nobel Prize in Chemistry 1994 George A. Olah Share this Facebook Twitter LinkedIn Email this page George A. Olah Facts George A. Olah Photo from the Nobel Foundation archive. George A. Olah The Nobel Prize in Chemistry 1994 Born: 22 May 1927, Budapest, Hungary Died: 8 March 2017, Los Angeles, CA, USA Affiliation at the time of the award: University of Southern California, Los Angeles, CA, USA Prize motivation: “for his contribution to carbocation chemistry” Prize share: 1/1 Work Chemical reactions in which molecules composed of atoms collide and form new compounds represent one of nature’s fundamental processes. Carbocations are electrically charged molecules in which the charge is concentrated on one carbon atom. They play an important role as intermediate stages in chemical reactions and have very short life spans. At the beginning of the 1960s, George Olah used very strong acids to produce carbocations in solution with life spans long enough so they could be studied. hemist George Olah, who won USC’s first Nobel prize, died at his home in Beverly Hills on March 8. He was 89. Olah had a profound influence on the world of hydrocarbon chemistry and his discoveries had great application to everyday life: He helped pave the way for less-polluting gasoline, more-effective oil refining and several modern drugs. At USC, he was the Distinguished Professor of Chemistry, Chemical Engineering and Materials Science, Donald P. and Katherine B. Loker Chair in Organic Chemistry and founding director of the Loker Hydrocarbon Research Institute in the USC Dornsife College of Letters, Arts and Sciences. “Distinguished Professor George Olah was a true legend in the field of chemistry. His pioneering research fundamentally redefined the field’s landscape and will influence its scholarly work for generations to come,” said USC President C. L. Max Nikias. “While Professor Olah was a world-renowned Nobel laureate and a giant in chemistry, he was also a beloved member of our Trojan Family. He will be deeply missed.” While Professor Olah was a world-renowned Nobel laureate and a giant in chemistry, he was also a beloved member of our Trojan Family. C. L. Max Nikias USC Provost Michael Quick praised Olah’s influential scholarship, as well as his generosity. “He was benevolent,” Quick said. “When he won the Nobel Prize in Chemistry in 1994, he said that while it was personally rewarding, he believed it was also recognition of his past and present students and associates whose work didn’t often receive notice.” Prize-winning legacy Olah received the 1994 Nobel Prize in Chemistry for groundbreaking work on superacids and his observations of what are known as carbocations, a fleeting chemical species long theorized to exist, but never confirmed — until Olah devised a way to keep them around long enough to study their properties. What he found revolutionized the understanding of organic chemistry, leading to new discoveries, new fields of research and countless applications. His discovery of how to make concentrated solutions of unusual hydrocarbon cations — using what he called “Magic Acids” — created an entire new field of chemistry of considerable theoretical and practical importance. The potent acids — billions or some cases even many trillions of times stronger than previously recognized “strong” acids such as concentrated sulfuric acid — can generate carbocations in solution that were previously thought to be impossible. Olah also investigated whether a similar but more general approach could be used to produce what are called electrophiles. These are reagents — compounds causing chemical reactions — that are attracted to electrons and are highly reactive. This resulted in the development of the concept of superelectrophilic activation and the study of superelectrophiles. His post-Nobel research focused not only on developing a promising new approach for solving long-range dependence on dwindling and nonrenewable fossil fuels, but also on mitigating global climate change caused by derived greenhouse gases such as carbon dioxide and methane. His novel approach — which he termed “the methanol economy” — was based on the use of methanol for energy storage as a convenient renewable liquid fuel to replace gasoline and diesel and as a feedstock for making petroleum-derived products. Origins of an influential career The chemist never claimed to have had a eureka moment in his research that led to his Nobel Prize. Instead, he credited long hours of laboratory routine that typically began just after dawn and continued until 10 at night. Upon winning the prize, he singled out for praise his longtime collaborator at USC Dornsife, Surya Prakash — George A. and Judith A. Olah Nobel Laureate Chair in Hydrocarbon Chemistry and professor of chemistry. Prakash went to Case Western Reserve University in 1974 as a 20-year-old PhD student to work with Olah and moved with him to USC in 1977 to help him establish the Loker Hydrocarbon Research Institute. In the years since, the institute has trained more than 300 scientists and has had countless patents and discoveries. Olah was instrumental to the institute’s tremendous growth. “The chemistry George did was very original, but on top of that, he was a very kind and generous man,” said Prakash, who today leads the institute. “In addition to bringing great credit to the chemistry department, he was one of the original pioneers who made this a great university: He brought scientific excellence and creativity to USC.” The chemistry George did was very original, but on top of that, he was a very kind and generous man. Surya Prakash USC Dornsife Dean Amber D. Miller noted Olah’s passing as a loss both to USC Dornsife and to the field of chemistry. “He was an academic luminary whose passion for the process of discovery invigorated our university community over his four decades of service,” Miller said. “As we mourn his loss, we also remember with gratitude that his pioneering research continues to inform new pathways for a sustainable future.” Olah was a firm believer in goal-oriented research, and his studies during his 40-year career at USC Dornsife were distinguished by their immense practical applications. He made significant contributions to the development of improved lead-free gasoline, cleaner high-octane gas and other promising nonpolluting fuels, as well as many chemical processes now used in pharmaceutical and industrial chemistry. His research also led to the development of a new kind of fuel cell, called the direct liquid methanol fuel cell, a highly efficient source of electricity. He developed new methods to convert existing natural gas (methane) directly and efficiently to methanol. However, the true methanol economy, Olah argued, will do without fossil fuels like natural gas, oil and coal, instead producing methanol by the reaction of hydrogen with carbon dioxide collected from exhaust gases from power plants and various industrial emissions. Eventually, Olah proposed, it will be possible to separate atmospheric carbon dioxide and convert it to methanol, enabling mankind to liberate itself from dependence on fossil fuels. This approach has the added advantage of diminishing the danger of global warming by removing and recycling the rising carbon dioxide content of the atmosphere. The substantial energy required to generate the needed hydrogen for methanol production could come from safe nuclear power plants and alternatives such as sunlight, wind and geothermal sources, he noted. The Renaissance man Olah was born in Budapest, Hungary, in 1927. He showed no interest in chemistry during his formative years. Instead, he followed a strict and demanding curriculum that heavily emphasized the humanities, including eight years of Latin and obligatory German and French. That stayed with him later in life, when he became known in academic circles as a Renaissance man. “He was very well-read,” Prakash said. “He knew history, he knew philosophy. He appreciated music and art. He was a voracious reader.” After high school, having survived the ravages of World War II in Budapest and perhaps cognizant of the difficulties of life in a small, war-torn country, he opted to study chemistry at the Technical University of Budapest. There he was particularly intrigued by organic chemistry, earning his doctoral degree in the subject and joining the faculty as assistant professor. Invited to join the newly established Central Research Institute of the Hungarian Academy of Sciences as head of department of organic chemistry and associate scientific director in 1954, Olah established a small research group, which now included his wife, Judith Lengyel, whom he married in 1949. However, after the Soviet military crackdown on the Hungarian Uprising of 1956, the future for Olah and his team looked bleak. Some 200,000 Hungarians fled their country in the final months of that year for a new life in the West. Olah, his wife and young son and much of his research group were among them. Brief stays in England and Canada were followed by their major move — to the United States. Olah became a scientist with Dow Chemical Co., which had recently established a small research laboratory in Michigan. At Dow, a major user of carbocationic chemistry, Olah began his initial work on stable carbocations. His work had practical significance, helping to improve some industrial processes, and he was promoted to company scientist, the highest research position without administrative responsibility. The move to academia In 1965, Olah joined Western Reserve University in Cleveland, Ohio, as a professor and department chair. There he was instrumental in merging the chemistry department with that of neighboring Case Institute of Technology in 1967. After 12 years in Cleveland, where his work earned him membership in the National Academy of Sciences, Olah moved to California to join USC. Some 14 members of his research group, with Prakash, accompanied him. He embraced the challenge of building up USC’s chemistry department — and he and his family fell in love with the Southern California lifestyle. Aware of the need for a long-range program of basic research and graduate education in the field of hydrocarbon chemistry, Olah became founding director of the Hydrocarbon Research Institute, which opened its doors in 1979, thanks to a generous donation from Donald Loker and his wife, Katherine Loker ’40. The institute was renamed in honor of the couple in 1984. Olah was determined that receiving the Nobel Prize would not significantly affect his life nor his research. He felt he was successful in that goal, noting that with the help of dedicated younger colleagues and associates and by close collaboration with Prakash, he was able not only to continue his research but also to extend it into new and challenging areas. Honors and prizes He was a fellow of the Royal Society and Canadian Royal Society and a member of the National Academy of Sciences, National Academy of Engineering, Italian and Hungarian academies of sciences, and the European Academy of Arts, Sciences and Humanities. In his native Hungary, he received awards ranging from the Semmelweis Budapest Award to the Széchenyi Grand Prize of Hungary. Olah also received honorary Doctor of Science degrees from the University of Sopron, Hungary and University of Munich, among others. Besides the Nobel, his many prizes included the 2013 Eric and Sheila Samson Prime Minister’s Prize for Innovation in Alternative Fuels for Transportation, the Priestley Medal from the American Chemical Society in 2005 and the USC Associates Award for Creativity in Research and Scholarship in 1985. During his career, Olah authored or co-authored 20 books and close to 1,500 scientific publications. He held 160 patents from seven countries, including four for the transformation of natural gas into gasoline-range hydrocarbons. He is survived by his wife, Judith Olah; their sons, George Olah Jr. ’89 MBA and Ronald Olah ’85 MD; daughters-in-law, Sally Olah and Cindy Olah; grandsons Peter Olah ’16 BS and Justin Olah; and granddaughter Kaitlyn Olah. Details of a USC campus celebration of Olah’s life are pending.
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