The Graz agreement was a proposed agreement made between the Bosnian Serb leader Radovan Karadžić and the Bosnian Croat leader Mate Boban on 6 May 1992 in the city of Graz, Austria. The agreement publicly declared the territorial division between Republika Srpska and the Croatian Community of Herzeg-Bosnia and called for an end of conflicts between Serbs and Croats. The largest group in Bosnia and Herzegovina, the Bosniaks, did not take part in the agreement and were purposefully not invited to the negotiations.

In their joint statement the Bosnian Croat and Serb leadership described it as a peace agreement. Croatian President Franjo Tuđman, in a letter to United States senator Robert Dole, later presented the agreement as part of a Conference on Bosnia and Herzegovina sponsored by the European Community. The parties ultimately parted ways without signing any agreement and clashes between Croat and Serb forces continued.

Meeting and aftermath
On 6 May 1992, the representatives of the Serbian community of BiH, Radovan Karadžić, Momčilo Krajišnik and Branko Simić, and the Croatian Community of BiH, represented by Mate Boban and Franjo Boras, met without Bosnian Muslim representatives in the city of Graz in Austria to discuss the future of Bosnia and Herzegovina. Mate Boban and Radovan Karadžić issued a joint statement on 6 May 1992, describing it as a peace agreement and called for a general cease-fire in BiH. The territorial demarcation of the two communities in BiH was to be based on the 1939 borders of Banovina of Croatia. It was agreed that "in defining the borderline between the two constituent units in the area of Kupres, as well as Bosanska Posavina [...] account should be taken of the compactness of areas and communications." However, an agreement was not reached for the strip of land along the banks of the Neretva, near Mostar, nor the town of Mostar, which is why the parties wanted the European Community to arbitrate their respective claims regarding these regions. The agreement concluded: "in view of this agreement, no more reasons obtain for an armed conflict between the Croatians and the Serbs in the entire territory of Bosnia and Herzegovina."

The parties ultimately parted ways on 6 May 1992, without signing any agreement, and clashes between Croat and Serb forces continued. As of May 1992, military cooperation was achieved between the Croatian Defence Council (HVO) and the Army of the Republic of Bosnia and Herzegovina (ARBiH) against Serb forces.

Reception
According to Vreme's military analyst Miloš Vasić the Graz agreement was "the single most important document of the war" and was meant to limit conflict between Serb and Croat forces by allowing both parties to concentrate on taking Bosniak territory from the Bosnian forces. The agreement was seen as Bosnian Croats betraying their Bosniak allies. It was also seen as a sequel to the Milošević-Tuđman Karađorđevo meeting by the ICTY judgement in the Blaškić case. A Washington Post editorial compared the agreement to the Hitler-Stalin pact that divided Poland.

In the ICTY case against Prlić et al., Herbert S. Okun was called to testify in April 2007. In this capacity as the deputy of Cyrus Vance, UN special envoy to the Balkans, he had attended a number of meetings where the division of Bosnia Herzegovina was discussed. As Okun described it, the aspirations of Croatia and Serbia for the annexation of parts of Bosnia and Herzegovina became evident after Tuđman and Milošević met in Karađorđevo in March 1991 and after the meeting of Mate Boban and Radovan Karadžić in May 1992 in Graz. Neither party kept their plans for the creation of separate states within Bosnia-Herzegovina and their annexation to Serbia and Croatia secret at their subsequent meetings with international diplomats. Herbert Okun testified that on May 6, 1992, Radovan Karadžić and Mate Boban met in Graz in Austria to discuss the partition of Bosnia and Herzegovina along the boundaries of the Croatian Banovina. Herbert Okun also testified that during the international conference on the former Yugoslavia, held between September 1992 and May 1993, Franjo Tuđman was the de facto president of the Bosnian Croat delegation, including, among others, Mate Boban and Milivoj Petković. During that conference, Herbert Okun heard Franjo Tuđman make statements about extending the borders of Croatia, either directly or by including Herceg-Bosna within Croatia. He also heard him make statements about his support for the government of Mate Boban.

The May 2013 ICTY judgement in the case discusses the joint statement made in Graz, as well as the subsequent Agreement on Friendship and Cooperation between Bosnia and Herzegovina and Croatia and the peace plans offered before and during the Bosnian War.

Notes

References

External links

Bosnian War
Treaties concluded in 1992
Treaties entered into force in 1992
Treaties of Bosnia and Herzegovina
May 1992 events in Europe
1992 in Austria
History of Graz

Graz agreement


Thure E. Cerling (born 1949) is a Distinguished Professor of Geology and Geophysics and a Distinguished Professor of Biology at the University of Utah. Cerling is a leading expert in the evolution of modern landscapes including modern mammals and their associated grassland ecologies and stable isotope analyses of the atmosphere. Cerling lives in Salt Lake City, Utah.

"A single hair can determine a person's location during the past weeks or even years" – Thure E. Cerling

Cerling's research interests are primarily focused on Earth surface geochemistry processes and on the geological record of ecological change. Particularly, working on conservation biology, Cerling has analyzed the modern animal diet and physiology by using stable isotopes as natural tracers as well as studying dietary changes of different mammalian lineages extending over millions of years.

Emphasizing continental ecologies of lakes and modern soils and ecosystems, Cerling has written extensievely about the evolution of ecosystems, the inception and strengthening of monsoons, and the atmosphere over geological time scales through evidence gathered about the fractionation of stable isotopes in these systems.

Current research work includes a focus on the development of landforms in semi-arid regions, the geology of Old World paleo-anthropologic sites and on contaminant migration in surface and ground waters, including the use of tritium and helium as hydrological tracers.

Together with James Ehleringer, he established the Stable Isotope Biogeochemistry and Ecology (IsoCamp) summer course at the University of Utah, which "trains students in the fundamental environmental and biological theory underlying isotope fractionation processes across a broad spectrum of ecological and environmental applications".

Early life

Thure E. Cerling received his Bachelor of Science degree in geology and chemistry from Iowa State University, in Ames, Iowa, in 1972, and, in 1973, his Master of Science in geology from Iowa State. In 1977 he was awarded a Ph.D. in geology from the University of California at Berkeley. From 1977 to 1979 he worked as a research scientist at Oak Ridge National Laboratory and, from 1979 he has been a member of the University of Utah's faculty.

Global ecological changes

With the publication of "Expansion of C4 ecosystems as an indicator of global ecological change in the late Miocene" in 1993, Cerling, helped by Yang Wang and Jay Quade, made relevant studies relatively to carbon isotopes. Thanks to a deep analysis of palaeovegetation from palaeosols and palaeodiet measured in fossil tooth enamel, was demonstrated a global increase in the biomass of plants using C4 photosynthesis between 7 and 5 million years ago. The decrease of atmospheric  concentrations over the history below a threshold that favored the C3-photosynthesizing plants was considered as a valid reason for the global expansion of C4 biomass.
The publication "Global vegetation change through the Miocene/Pliocene boundary" in 1997 confirmed these results, demonstrating even how at lower latitudes the change appeared to occur earlier because of the threshold for C3 photosynthesis is higher at warmer temperatures.

Give me a hair and I'll tell you where you have been.

Thure Cerling and James Ehleringer, a biology professor at the University of Utah, founded Isoforensics in 2003, a company with the aim of interpreting the stable isotope composition of various biological and synthetic materials. This was the first step for the discovery they made which was first published on February 25, 2008, by the "Proceedings of the National Academy of Sciences" with the title "Hydrogen and oxygen isotope ratios in human hair are related to geography".
To know where people have been and where they lived for a while are information that became available by analyzing the stable isotope composition of their scalp hair. Cerling discovered that a strand of hair could provide valuable clues about a person's travels by studying the variation of hydrogen-2 (δ2H) and oxygen-18 (δ18O) isotopes and comparing them to the ones in the drinking water. The extent of the information that can be deduced depends on the length of the hair: the longer is the hair, the greater is the extraction of information. The variation with geography of isotope concentrations is linked with precipitations, cloud temperatures and with the amount of water that evaporates from soil and plants. When clouds move off the ocean towards inland the ratios of oxygen-18 to oxygen-16 and hydrogen-2 to hydrogen-1 tend to decrease because of the rain water with oxygen-18 and hydrogen-2, being heavier, tends to fall first.
Samples of tap water were collected from more than 600 cities across the United States as well as hair samples from the barbershops in 65 cities in 20 states. The comparison showed that both hair and drinking water samples had the same isotopic variations. In order to display these information, the scientists produced color-coded maps based on the correlation of the isotopes in hair to those in drinking water. This maps show how ratios of hydrogen and oxygen isotopes in scalp hair vary in different areas of the United States. It was so proved that the water drank by a human being leaves in the hair an evidence which contain oxygen and hydrogen isotopes equal to the ones in the tap water.
This technique would have been a new tool for policemen, anthropologists, archaeologists and doctors.

The elephant tail hair: how many things they can say!

Professor Cerling, helped by James Ehleringer and Christopher Remien (two University of Utah colleagues), George Wittemyer of Colorado State University and member of "Save the Elephants" in Nairobi, and Iain Douglas-Hamilton, who founded the association "Save the Elephants", conducted a research around the Samburu and Buffalo Springs national reserves in northern Kenya analyzing carbon and other stable isotopes in elephant tail hair to discover where and what Victoria, Anastasia and Cleopatra, three daughters of a mother elephant named Queen Elizabeth, usually eat over a six-years period (2000–2006). In order to monitor their life, the elephants were equipped with a Global Positioning System that recorded their positions every hour for the whole research period. For getting the sample of tail hair, elephants were immobilized with drug-filled dart guns when necessary. Considering that the hair grows about an inch per month, a single hair contained isotopic information to diet during an 18-month period.

Wet and dry seasons: different responses

The analysis of ratios of carbon-13 to carbon-12 along the length of a single elephant hair led Cerling and his crew to understand the elephants' diet. During the wet season, after the grass had grown long enough for elephants to grab with their trunks, their tail hair showed the presence of different form of carbon, indicating a high amount of high-protein grass. On the other hand, during the dry season, the results obtained by the analysis of the hair pointed out how elephants had switched over to shrubs and trees.

Birth and Cattle

For what concern the Samburu-Buffalo Springs, five weeks after the rainy season had started, the grass became rich in nutrients and the females were most likely to conceive, giving birth 22 months later, just in time for another rainy season to provide nutrients to the grass they would have eaten: the cycle could restart.
The research also pointed out how developed is the competition between elephants and cattle: during the typical wet season diet of elephants, the overgrazing by cattle caused the grass to be very short, resulting in a limited access to it for elephants, out-competing them. This situation could have influenced the elephants' ability to bulk up for pregnancy.

Behavior

All these analyses pointed out even that there are some elephant families friendlier than others and showed how there are dominant families that settle down in the best places, where there is plenty of food and water.

Publications by Cerling

 Thure Cerling; Iain Douglas-Hamilton; Lee Siegel: "Elephant Tracks" University of Utah News Release, January 2, 2006.

References

External links

1949 births
Living people
Geochemistry
Members of the United States National Academy of Sciences
Fellows of the American Association for the Advancement of Science
University of Utah faculty
Iowa State University alumni
UC Berkeley College of Letters and Science alumni
Oak Ridge National Laboratory people

Thure E. Cerling


Sophia Giustina Dussek (née Corri; later Moralt; Edinburgh, 1 May 1775 – London, ca. 1831) was a Scottish singer, pianist, harpist, and composer of Italian descent.

In 1792, Dussek married the composer Jan Ladislav Dussek. Following Jan's death in 1812, Sophia married the violist John Alvis Moralt. The couple lived in Paddington, where she founded a music school.

The opus 2 sonatas were published in at least 3 editions in the 1790s by the Corri-Dussek company in London as by Madame Dussek, and there is no reason to doubt that the 6 sonatas of opus 2, including the famous C minor sonata published and misattributed by Schott as by JL, are anything but the work of Sophia. Paris editions of opus 2 published by Pleyel only bear the name Dussek, leading Zabaleta to his misattribution, but nobody actually claimed opus 2 as the work of JL rather than Dussek before the mid-20th century.

Life and family

Sophia Dussek was born into the Corri family. She studied voice with her father, composer, music publisher, and impresario Domenico Corri. Her uncle was composer Natale Corri and her cousin was soprano Fanny Corri-Paltoni. Her father provided Sophia with vocal instruction and had her performing from a young age. She was well known as a soprano and composer of songs.

After moving to London in 1788, she studied with Luigi Marchesi and Giovanni Battista Cimador. Dussek was a highly accomplished performer and she had her London debut at the prestigious Salomon concerts in 1791 with Haydn directing from the harpsichord, and afterwards sang quite a bit of the series, taking part in the first performance of Haydn's The Storm. In 1792, she sang the lead in the premiere of Harriet Wainwright's opera Comala.

She also played a big role in the introduction of Mozart's music to London. She was a soloist in the London premiere of the Requiem, given at John Ashley's Lenten Oratorios, Covent Garden, on 20 February 1801. In 1792 she married Jan Ladislav Dussek. She had been performing, singing and playing the piano and harp with him for some time before that. Their daughter, Olivia, was also a pianist, harpist, and composer.

In 1796, Sophia began having serious marital troubles with her husband. In an account of uncertain veracity, it was reported that Sophia, who had fallen in love with another man, asked Dussek for money to repair her harp. She then used the money to leave the house, removing her belongings in her harp case, and claiming to have left for dinner with a female friend. A suspicious Dussek went with his father-in-law to the man's house, where Sophia locked herself in. She and Dussek argued, and she cursed him, claiming to be pregnant by the other man. Dussek, relenting, promised her freedom to do what she wanted; this led to a reconciliation of sorts.

Sophia had to wait until she knew Dussek had died before she could remarry. After Jan Ladislav's death in 1812 Sophia married the viola player John Alvis Moralt. They lived in Paddington, where she established a music school. She published sonatas, rondos, variations, and numerous arrangements for the piano or harp.

Works list
Keyboard
 Sonata for pianoforte (harpsichord) with violin or flute, Op. 1 (London, ca. 1793)
 3 Sonatas for harpsichord (pianoforte) with violin, Op. 1 (Paris)
 Sonata for pianoforte (London, ca. 1805)
Keyboard or Harp
 The New German Waltz - adapted as a Rondo for Harp or Piano Forte (1799)
Harp
 3 Sonatas with Scots Airs and Reels for the Adagios & Rondos, Op. 2 (Book I): B-flat, G, C minor (London, Corri & Co., 1794)
 3 Sonatas with Scots Airs and Reels for the Adagios & Rondos, Op. 2 (Book II): E-flat, F, C (London, Corri & Co., 1795)

 A French air with variations (London, Chappel & Co., 1820)
 "C'est l'amour": A 3rd French air with variations (London, Chappel & Co., 1820)
 Introduction and March (London, 1822)
 Variations on God Save the King (London, 1822)
 "La Chasse": An original rondo (London, Chappel & Co., 1824)
 at least 7 sets of Favorite Airs (London), some with flute or violin ad libitum
 arrangements
Harp and piano
 Duett (London, ca. 1812)
 Introduction and Waltz (London, 1822)
 arrangements

Editions
 Sophia Corri. Main Works for Solo Harp: 6 Sonatas Op. 2 / French Air / C'est l'Amour / La Chasse. Ed. Floraleda Sacchi. Ut Orpheus Edizioni, 2010,

Selected discography
 Sophia Giustona Corri: Works for solo harp. Includes six Sonatas. Performed (on historical instrument) by Floraleda Sacchi (Tactus Records, 2009, TC.772801)
 Sophia Corri Dussek: Works for solo harp. Includes six Sonatas. Performed (on historical instrument) by Floraleda Sacchi (Amadeus Arte, 2011, AAP11006)
 Sophia Corri-Dussek: works for harp & piano. Includes Piano sonata in A major. Performed (on historical instruments) by Floraleda Sacchi and Marco Cadario (Amadeus Arte, 2011, AAP11007)
 Madame et Monsieur Dussek: harp sonatas, sonatinas and pieces performed (on historical instrument) by Masumi Nagasawa (Etcetera Records, 2012, KTC 1439)
 Jan Ladislav Dussek. Duos for harp & pianoforte: Sophia's Introduction & waltz performed (on historical instruments) by Masumi Nagasawa & Richard Egarr (Etcetera Records, 2012, KTC 1436)
Dussek, Jan Ladislav & Sophia: Harp sonatas by Kyunghee Kim-Sutre (Sonarti records, 2013, RT01)

Notes

References

External links

3 Harp Sonatas, Op.2 Score by MUSOPEN
3 Favorite Airs, Set 2 Score by MUSOPEN
3 Favorite Airs with Variations for the Harp, Set 1 Score by MUSOPEN
Advanced Wikipedia page of Sophia Dussek (As Sophia Corri)

1775 births
1830s deaths
18th-century British composers
18th-century British women opera singers
18th-century classical composers
18th-century Scottish women singers
19th-century British composers
19th-century Scottish women opera singers
19th-century classical composers
British Romantic composers
Scottish women classical composers
Italian British musicians
Musicians from Edinburgh
Scottish classical composers
Scottish classical pianists
Scottish women pianists
Scottish harpists
Women harpists
Scottish people of Italian descent
Women classical pianists
19th-century women composers
18th-century women composers
19th-century women pianists

Sophia Dussek


Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins.  Only these 22 appear in the genetic code of all life.

Amino acids can be classified according to the locations of the core structural functional groups, as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, ionization, and side chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid residues form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life on Earth and its emergence.

Amino acids are formally named by the IUPAC-IUBMB Joint Commission on Biochemical Nomenclature in terms of the fictitious "neutral" structure shown in the illustration. For example, the systematic name of alanine is 2-aminopropanoic acid, based on the formula . The Commission justified this approach as follows:

The systematic names and formulas given refer to hypothetical forms in which amino groups are unprotonated and carboxyl groups are undissociated. This convention is useful to avoid various nomenclatural problems but should not be taken to imply that these structures represent an appreciable fraction of the amino-acid molecules.

History

The first few amino acids were discovered in the early 1800s. In 1806, French chemists Louis-Nicolas Vauquelin and Pierre Jean Robiquet isolated a compound from asparagus that was subsequently named asparagine, the first amino acid to be discovered. Cystine was discovered in 1810, although its monomer, cysteine, remained undiscovered until 1884. Glycine and leucine were discovered in 1820. The last of the 20 common amino acids to be discovered was threonine in 1935 by William Cumming Rose, who also determined the essential amino acids and established the minimum daily requirements of all amino acids for optimal growth.

The unity of the chemical category was recognized by Wurtz in 1865, but he gave no particular name to it. The first use of the term "amino acid" in the English language dates from 1898, while the German term, , was used earlier. Proteins were found to yield amino acids after enzymatic digestion or acid hydrolysis. In 1902, Emil Fischer and Franz Hofmeister independently proposed that proteins are formed from many amino acids, whereby bonds are formed between the amino group of one amino acid with the carboxyl group of another, resulting in a linear structure that Fischer termed "peptide".

General structure

Amino acids are known as 2-, alpha-, or α-amino acids..  They have the generic formula  in most cases, where R is an organic substituent known as a "side chain".

Of the many hundreds of amino acids, 22 are proteinogenic ("protein-building"). It is these 22 compounds that combine to give a vast array of peptides and proteins.

Chirality
The carbon atom next to the carboxyl group is called the α–carbon. It bears the amine and, except in the case of glycine, the R group or side chain specific to each amino acid.  With four distinct substituents, the α–carbon is stereogenic (gives rise to chirality) in all amino acids except glycine. All proteogenic amino acids have the L configuration.  They are "left-handed" enantiomers, which refers to the stereoisomers of the alpha carbon.

A few D-amino acids ("right-handed") have been found in nature, e.g.,  in bacterial envelopes, as a neuromodulator (D-serine), and in some antibiotics. Rarely, D-amino acid residues are found in proteins, and are converted from the -amino acid as a post-translational modification.

Side chains

Charged side chains

Five amino acids possess a charge at neutral pH. Often these side chains appear at the surfaces on proteins to enable their solubility in water, and side chains with opposite charges form important electrostatic contacts called salt bridges that maintain structures within a single protein or between interfacing proteins. Many proteins bind metal into their structures specifically, and these interactions are commonly mediated by charged side chains such as aspartate, glutamate and histidine.

The two negatively charged amino acids at neutral pH are aspartate (Asp, D) and glutamate (Glu, E). The anionic carboxylate groups behave as Brønsted bases in most circumstances. Enzymes in very low pH environments, like the aspartic protease pepsin in mammalian stomachs, may have catalytic aspartate or glutamate residues that act as Brønsted acids.

There are three amino acids with side chains that are cations at neutral pH: arginine (Arg, R), lysine (Lys, K) and histidine (His, H). Arginine has a charged guanidino group and lysine a charged alkyl amino group, and are fully protonated at pH 7. Histidine's imidazole group has a pKa of 6.0, and is only around 10 % protonated at neutral pH. Because histidine is easily found in its basic and conjugate acid forms it often participates in catalytic proton transfers in enzyme reactions.

Polar uncharged side chains

The polar, uncharged amino acids serine (Ser, S), threonine (Thr, T), asparagine (Asn, N) and glutamine (Gln, Q) readily form hydrogen bonds with water and other amino acids. They do not ionize in normal conditions, a prominent exception being the catalytic serine in serine proteases. This is an example of severe perturbation, and is not characteristic of serine residues in general. Threonine has two chiral centers, not only the L (2S) chiral center at the α-carbon shared by all amino acids apart from achiral glycine, but also (3R) at the β-carbon. The full stereochemical specification is (2S,3R)-L-threonine.

Hydrophobic side chains

Nonpolar amino acid interactions are the primary driving force behind the processes that fold proteins into their functional three dimensional structures. None of these amino acids' side chains ionize easily, and therefore do not have pKas, with the exception of tyrosine (Tyr, Y). The hydroxyl of tyrosine can deprotonate at high pH forming the negatively charged phenolate. Because of this one could place tyrosine into the polar, uncharged amino acid category, but its very low solubility in water matches the characteristics of hydrophobic amino acids well.

Special case side chains

Several side chains are not described well by the charged, polar and hydrophobic categories. Glycine (Gly, G) could be considered a polar amino acid since its small size means that its solubility is largely determined by the amino and carboxylate groups. However, the lack of any side chain provides glycine with a unique flexibility among amino acids with large ramifications to protein folding. Cysteine (Cys, C) can also form hydrogen bonds readily, which would place it in the polar amino acid category, though it can often be found in protein structures forming covalent bonds, called disulphide bonds, with other cysteines. These bonds influence the folding and stability of proteins, and are essential in the formation of antibodies. Proline (Pro, P) has an alkyl side chain and could be considered hydrophobic, but because the side chain joins back onto the alpha amino group it becomes particularly inflexible when incorporated into proteins. Similar to glycine this influences protein structure in a way unique among amino acids. Selenocysteine (Sec, U) is a rare amino acid not directly encoded by DNA, but is incorporated into proteins via the ribosome. Selenocysteine has a lower redox potential compared to the similar cysteine, and participates in several unique enzymatic reactions. Pyrrolysine (Pyl, O) is another amino acid not encoded in DNA, but synthesized into protein by ribosomes. It is found in archaeal species where it participates in the catalytic activity of several methyltransferases.

β- and γ-amino acids
Amino acids with the structure , such as β-alanine, a component of carnosine and a few other peptides, are β-amino acids. Ones with the structure  are γ-amino acids, and so on, where X and Y are two substituents (one of which is normally H).

Zwitterions

The common natural forms of amino acids have a zwitterionic structure, with  ( in the case of proline) and  functional groups attached to the same C atom, and are thus α-amino acids. and are the only ones found in proteins during translation in the ribosome.
In aqueous solution at pH close to neutrality, amino acids exist as zwitterions, i.e. as dipolar ions with both  and  in charged states, so the overall structure is . At physiological pH the so-called "neutral forms"  are not present to any measurable degree. Although the two charges in the zwitterion structure add up to zero it is misleading to call a species with a net charge of zero "uncharged".

In strongly acidic conditions (pH below 3), the carboxylate group becomes protonated and the structure becomes an ammonio carboxylic acid, . This is relevant for enzymes like pepsin that are active in acidic environments such as the mammalian stomach and lysosomes, but does not significantly apply to intracellular enzymes. In highly basic conditions (pH greater than 10, not normally seen in physiological conditions), the ammonio group is deprotonated to give .

Although various definitions of acids and bases are used in chemistry, the only one that is useful for chemistry in aqueous solution is that of Brønsted: an acid is a species that can donate a proton to another species, and a base is one that can accept a proton. This criterion is used to label the groups in the above illustration. The carboxylate side chains of aspartate and glutamate residues are the principal Brønsted bases in proteins. Likewise, lysine, tyrosine and cysteine will typically act as a Brønsted acid. Histidine under these conditions can act both as a Brønsted acid and a base.

Isoelectric point

For amino acids with uncharged side-chains the zwitterion predominates at pH values between the two pKa values, but coexists in equilibrium with small amounts of net negative and net positive ions. At the midpoint between the two pKa values, the trace amount of net negative and trace of net positive ions balance, so that average net charge of all forms present is zero. This pH is known as the isoelectric point pI, so pI = (pKa1 + pKa2).

For amino acids with charged side chains, the pKa of the side chain is involved. Thus for aspartate or glutamate with negative side chains, the terminal amino group is essentially entirely in the charged form , but this positive charge needs to be balanced by the state with just one C-terminal carboxylate group is negatively charged. This occurs halfway between the two carboxylate pKa values: pI = (pKa1 + pKa(R)), where pKa(R) is the side chain pKa.

Similar considerations apply to other amino acids with ionizable side-chains, including not only glutamate (similar to aspartate), but also cysteine, histidine, lysine, tyrosine and arginine with positive side chains.

Amino acids have zero mobility in electrophoresis at their isoelectric point, although this behaviour is more usually exploited for peptides and proteins than single amino acids. Zwitterions have minimum solubility at their isoelectric point, and some amino acids (in particular, with nonpolar side chains) can be isolated by precipitation from water by adjusting the pH to the required isoelectric point.

Physicochemical properties
The 20 canonical amino acids can be classified according to their properties. Important factors are charge, hydrophilicity or hydrophobicity, size, and functional groups. These properties influence protein structure and protein–protein interactions. The water-soluble proteins tend to have their hydrophobic residues (Leu, Ile, Val, Phe, and Trp) buried in the middle of the protein, whereas hydrophilic side chains are exposed to the aqueous solvent. (In biochemistry, a residue refers to a specific monomer within the polymeric chain of a polysaccharide, protein or nucleic acid.) The integral membrane proteins tend to have outer rings of exposed hydrophobic amino acids that anchor them in the lipid bilayer. Some peripheral membrane proteins have a patch of hydrophobic amino acids on their surface that sticks to the membrane. In a similar fashion, proteins that have to bind to positively charged molecules have surfaces rich in negatively charged amino acids such as glutamate and aspartate, while proteins binding to negatively charged molecules have surfaces rich in positively charged amino acids like lysine and arginine. For example, lysine and arginine are present in large amounts in the low-complexity regions of nucleic-acid binding proteins. There are various hydrophobicity scales of amino acid residues.

Some amino acids have special properties. Cysteine can form covalent disulfide bonds to other cysteine residues. Proline forms a cycle to the polypeptide backbone, and glycine is more flexible than other amino acids.

Glycine and proline are strongly present within low complexity regions of both eukaryotic and prokaryotic proteins, whereas the opposite is the case with cysteine, phenylalanine, tryptophan, methionine, valine, leucine, isoleucine, which are highly reactive, or complex, or hydrophobic.

Many proteins undergo a range of posttranslational modifications, whereby additional chemical groups are attached to the amino acid residue side chains sometimes producing lipoproteins (that are hydrophobic), or glycoproteins (that are hydrophilic) allowing the protein to attach temporarily to a membrane. For example, a signaling protein can attach and then detach from a cell membrane, because it contains cysteine residues that can have the fatty acid palmitic acid added to them and subsequently removed.

Table of standard amino acid abbreviations and properties

Although one-letter symbols are included in the table, IUPAC–IUBMB recommend that "Use of the one-letter symbols should be restricted to the comparison of long sequences".

Two additional amino acids are in some species coded for by codons that are usually interpreted as stop codons:

In addition to the specific amino acid codes, placeholders are used in cases where chemical or crystallographic analysis of a peptide or protein cannot conclusively determine the identity of a residue. They are also used to summarise conserved protein sequence motifs. The use of single letters to indicate sets of similar residues is similar to the use of abbreviation codes for degenerate bases.

Unk is sometimes used instead of Xaa, but is less standard.

Ter or * (from termination) is used in notation for mutations in proteins when a stop codon occurs. It corresponds to no amino acid at all.

In addition, many nonstandard amino acids have a specific code. For example, several peptide drugs, such as Bortezomib and MG132, are artificially synthesized and retain their protecting groups, which have specific codes. Bortezomib is Pyz–Phe–boroLeu, and MG132 is Z–Leu–Leu–Leu–al. To aid in the analysis of protein structure, photo-reactive amino acid analogs are available. These include photoleucine (pLeu) and photomethionine (pMet).

Occurrence and functions in biochemistry

Proteinogenic amino acids

Amino acids are the precursors to proteins.  They join by condensation reactions to form short polymer chains called peptides or longer chains called either polypeptides or proteins. These chains are linear and unbranched, with each amino acid residue within the chain attached to two neighboring amino acids. In Nature, the process of making proteins encoded by DNA/RNA genetic material is called translation and involves the step-by-step addition of amino acids to a growing protein chain by a ribozyme that is called a ribosome. The order in which the amino acids are added is read through the genetic code from an mRNA template, which is an RNA copy of one of the organism's genes.

Twenty-two amino acids are naturally incorporated into polypeptides and are called proteinogenic or natural amino acids. Of these, 20 are encoded by the universal genetic code. The remaining 2, selenocysteine and pyrrolysine, are incorporated into proteins by unique synthetic mechanisms. Selenocysteine is incorporated when the mRNA being translated includes a SECIS element, which causes the UGA codon to encode selenocysteine instead of a stop codon. Pyrrolysine is used by some methanogenic archaea in enzymes that they use to produce methane. It is coded for with the codon UAG, which is normally a stop codon in other organisms. This UAG codon is followed by a PYLIS downstream sequence.

Several independent evolutionary studies have suggested that Gly, Ala, Asp, Val, Ser, Pro, Glu, Leu, Thr may belong to a group of amino acids that constituted the early genetic code, whereas Cys, Met, Tyr, Trp, His, Phe may belong to a group of amino acids that constituted later additions of the genetic code.

Standard vs nonstandard amino acids

The 20 amino acids that are encoded directly by the codons of the universal genetic code are called standard or canonical amino acids. A modified form of methionine (N-formylmethionine) is often incorporated in place of methionine as the initial amino acid of proteins in bacteria, mitochondria and chloroplasts. Other amino acids are called nonstandard or non-canonical. Most of the nonstandard amino acids are also non-proteinogenic (i.e. they cannot be incorporated into proteins during translation), but two of them are proteinogenic, as they can be incorporated translationally into proteins by exploiting information not encoded in the universal genetic code.

The two nonstandard proteinogenic amino acids are selenocysteine (present in many non-eukaryotes as well as most eukaryotes, but not coded directly by DNA) and pyrrolysine (found only in some archaea and at least one bacterium). The incorporation of these nonstandard amino acids is rare. For example, 25 human proteins include selenocysteine in their primary structure, and the structurally characterized enzymes (selenoenzymes) employ selenocysteine as the catalytic moiety in their active sites. Pyrrolysine and selenocysteine are encoded via variant codons. For example, selenocysteine is encoded by stop codon and SECIS element.

N-formylmethionine (which is often the initial amino acid of proteins in bacteria, mitochondria, and chloroplasts) is generally considered as a form of methionine rather than as a separate proteinogenic amino acid. Codon–tRNA combinations not found in nature can also be used to "expand" the genetic code and form novel proteins known as alloproteins incorporating non-proteinogenic amino acids.

Non-proteinogenic amino acids

Aside from the 22 proteinogenic amino acids, many non-proteinogenic amino acids are known. Those either are not found in proteins (for example carnitine, GABA, levothyroxine) or are not produced directly and in isolation by standard cellular machinery. For example, hydroxyproline , is synthesised from proline. Another example is selenomethionine).

Non-proteinogenic amino acids that are found in proteins are formed by post-translational modification. Such modifications can also determine the localization of the protein, e.g., the addition of long hydrophobic groups can cause a protein to bind to a phospholipid membrane.Examples:
the carboxylation of glutamate allows for better binding of calcium cations,
Hydroxyproline, generated by hydroxylation of proline, is a major component of the connective tissue collagen.
 Hypusine in the translation initiation factor EIF5A, contains a modification of lysine.

Some non-proteinogenic amino acids are not found in proteins. Examples include 2-aminoisobutyric acid and the neurotransmitter gamma-aminobutyric acid. Non-proteinogenic amino acids often occur as intermediates in the metabolic pathways for standard amino acids – for example, ornithine and citrulline occur in the urea cycle, part of amino acid catabolism (see below). A rare exception to the dominance of α-amino acids in biology is the β-amino acid beta alanine (3-aminopropanoic acid), which is used in plants and microorganisms in the synthesis of pantothenic acid (vitamin B5), a component of coenzyme A.

In mammalian nutrition

Amino acids are not typical component of food: animals eat proteins.  The protein is broken down into amino acids in the process of digestion.  They are then used to synthesize new proteins, other biomolecules, or are oxidized to urea and carbon dioxide as a source of energy. The oxidation pathway starts with the removal of the amino group by a transaminase; the amino group is then fed into the urea cycle. The other product of transamidation is a keto acid that enters the citric acid cycle. Glucogenic amino acids can also be converted into glucose, through gluconeogenesis.

Of the 20 standard amino acids, nine (His, Ile, Leu, Lys, Met, Phe, Thr, Trp and Val) are called essential amino acids because the human body cannot synthesize them from other compounds at the level needed for normal growth, so they must be obtained from food.

Semi-essential and conditionally essential amino acids, and juvenile requirements
In addition, cysteine, tyrosine, and arginine are considered semiessential amino acids, and taurine a semi-essential aminosulfonic acid in children. Some amino acids are conditionally essential for certain ages or medical conditions. Essential amino acids may also vary from species to species. The metabolic pathways that synthesize these monomers are not fully developed.

Non-protein functions

Many proteinogenic and non-proteinogenic amino acids have biological functions beyond being precursors to proteins and peptides.In humans, amino acids also have important roles in diverse biosynthetic pathways.  Defenses against herbivores in plants sometimes employ amino acids. Examples:

Standard amino acids
 Tryptophan is a precursor of the neurotransmitter serotonin.
 Tyrosine (and its precursor phenylalanine) are precursors of the catecholamine neurotransmitters dopamine, epinephrine and norepinephrine and various trace amines.
 Phenylalanine is a precursor of phenethylamine and tyrosine in humans. In plants, it is a precursor of various phenylpropanoids, which are important in plant metabolism.
 Glycine is a precursor of porphyrins such as heme.
 Arginine is a precursor of nitric oxide.
 Ornithine and S-adenosylmethionine are precursors of polyamines.
 Aspartate, glycine, and glutamine are precursors of nucleotides. However, not all of the functions of other abundant nonstandard amino acids are known.

Roles for nonstandard amino acids
Carnitine is used in lipid transport.
gamma-aminobutyric acid is a neurotransmitter.
5-HTP (5-hydroxytryptophan) is used for experimental treatment of depression.
L-DOPA (L-dihydroxyphenylalanine) for Parkinson's treatment,
Eflornithine inhibits ornithine decarboxylase and used in the treatment of sleeping sickness.
Canavanine, an analogue of arginine found in many legumes is an antifeedant, protecting the plant from predators.
Mimosine found in some legumes, is another possible antifeedant. This compound is an analogue of tyrosine and can poison animals that graze on these plants.

Uses in industry

Animal feed
Amino acids are sometimes added to animal feed because some of the components of these feeds, such as soybeans, have low levels of some of the essential amino acids, especially of lysine, methionine, threonine, and tryptophan. Likewise amino acids are used to chelate metal cations in order to improve the absorption of minerals from feed supplements.

Food
The food industry is a major consumer of amino acids, especially glutamic acid, which is used as a flavor enhancer, and aspartame (aspartylphenylalanine 1-methyl ester), which is used as an artificial sweetener. Amino acids are sometimes added to food by manufacturers to alleviate symptoms of mineral deficiencies, such as anemia, by improving mineral absorption and reducing negative side effects from inorganic mineral supplementation.

Chemical building blocks

Amino acids are low-cost feedstocks used in chiral pool synthesis as enantiomerically pure building blocks.

Amino acids are used in the synthesis of some cosmetics.

Aspirational uses

Fertilizer
The chelating ability of amino acids is sometimes used in fertilizers to facilitate the delivery of minerals to plants in order to correct mineral deficiencies, such as iron chlorosis. These fertilizers are also used to prevent deficiencies from occurring and to improve the overall health of the plants.

Biodegradable plastics

Amino acids have been considered as components of biodegradable polymers, which have applications as environmentally friendly packaging and in medicine in drug delivery and the construction of prosthetic implants. An interesting example of such materials is polyaspartate, a water-soluble biodegradable polymer that may have applications in disposable diapers and agriculture. Due to its solubility and ability to chelate metal ions, polyaspartate is also being used as a biodegradable antiscaling agent and a corrosion inhibitor.

Synthesis

Chemical synthesis
The commercial production of amino acids usually relies on mutant bacteria that overproduce individual amino acids using glucose as a carbon source. Some amino acids are produced by enzymatic conversions of synthetic intermediates. 2-Aminothiazoline-4-carboxylic acid is an intermediate in one industrial synthesis of L-cysteine for example. Aspartic acid is produced by the addition of ammonia to fumarate using a lyase.

Biosynthesis
In plants, nitrogen is first assimilated into organic compounds in the form of glutamate, formed from alpha-ketoglutarate and ammonia in the mitochondrion. For other amino acids, plants use transaminases to move the amino group from glutamate to another alpha-keto acid. For example, aspartate aminotransferase converts glutamate and oxaloacetate to alpha-ketoglutarate and aspartate. Other organisms use transaminases for amino acid synthesis, too.

Nonstandard amino acids are usually formed through modifications to standard amino acids. For example, homocysteine is formed through the transsulfuration pathway or by the demethylation of methionine via the intermediate metabolite S-adenosylmethionine, while hydroxyproline is made by a post translational modification of proline.

Microorganisms and plants synthesize many uncommon amino acids. For example, some microbes make 2-aminoisobutyric acid and lanthionine, which is a sulfide-bridged derivative of alanine. Both of these amino acids are found in peptidic lantibiotics such as alamethicin. However, in plants, 1-aminocyclopropane-1-carboxylic acid is a small disubstituted cyclic amino acid that is an intermediate in the production of the plant hormone ethylene.

Primordial synthesis
The formation of amino acids and peptides are assumed to precede and perhaps induce the emergence of life on earth. Amino acids can form from simple precursors under various conditions. Surface-based chemical metabolism of amino acids and very small compounds may have led to the build-up of amino acids, coenzymes and phosphate-based small carbon molecules. Amino acids and similar building blocks could have been elaborated into proto-peptides, with peptides being considered key players in the origin of life.

In the famous Urey-Miller experiment, the passage of an electric arc through a mixture of methane, hydrogen, and ammonia produces a large number of amino acids. Since then, scientists have discovered a range of ways and components by which the potentially prebiotic formation and chemical evolution of peptides may have occurred, such as condensing agents, the design of self-replicating peptides and a number of non-enzymatic mechanisms by which amino acids could have emerged and elaborated into peptides. Several hypotheses invoke the Strecker synthesis whereby hydrogen cyanide, simple aldehydes, ammonia, and water produce amino acids.

According to a review, amino acids, and even peptides, "turn up fairly regularly in the various experimental broths that have been allowed to be cooked from simple chemicals. This is because nucleotides are far more difficult to synthesize chemically than amino acids." For a chronological order, it suggests that there must have been a 'protein world' or at least a 'polypeptide world', possibly later followed by the 'RNA world' and the 'DNA world'. Codon–amino acids mappings may be the biological information system at the primordial origin of life on Earth. While amino acids and consequently simple peptides must have formed under different experimentally probed geochemical scenarios, the transition from an abiotic world to the first life forms is to a large extent still unresolved.

Reactions

Amino acids undergo the reactions expected of the constituent functional groups.

Peptide bond formation

As both the amine and carboxylic acid groups of amino acids can react to form amide bonds, one amino acid molecule can react with another and become joined through an amide linkage. This polymerization of amino acids is what creates proteins. This condensation reaction yields the newly formed peptide bond and a molecule of water. In cells, this reaction does not occur directly; instead, the amino acid is first activated by attachment to a transfer RNA molecule through an ester bond. This aminoacyl-tRNA is produced in an ATP-dependent reaction carried out by an aminoacyl tRNA synthetase. This aminoacyl-tRNA is then a substrate for the ribosome, which catalyzes the attack of the amino group of the elongating protein chain on the ester bond. As a result of this mechanism, all proteins made by ribosomes are synthesized starting at their N-terminus and moving toward their C-terminus.

However, not all peptide bonds are formed in this way. In a few cases, peptides are synthesized by specific enzymes. For example, the tripeptide glutathione is an essential part of the defenses of cells against oxidative stress. This peptide is synthesized in two steps from free amino acids. In the first step, gamma-glutamylcysteine synthetase condenses cysteine and glutamate through a peptide bond formed between the side chain carboxyl of the glutamate (the gamma carbon of this side chain) and the amino group of the cysteine. This dipeptide is then condensed with glycine by glutathione synthetase to form glutathione.

In chemistry, peptides are synthesized by a variety of reactions. One of the most-used in solid-phase peptide synthesis uses the aromatic oxime derivatives of amino acids as activated units. These are added in sequence onto the growing peptide chain, which is attached to a solid resin support. Libraries of peptides are used in drug discovery through high-throughput screening.

The combination of functional groups allow amino acids to be effective polydentate ligands for metal–amino acid chelates.
The multiple side chains of amino acids can also undergo chemical reactions.

Catabolism

Degradation of an amino acid often involves deamination by moving its amino group to alpha-ketoglutarate, forming glutamate. This process involves transaminases, often the same as those used in amination during synthesis. In many vertebrates, the amino group is then removed through the urea cycle and is excreted in the form of urea. However, amino acid degradation can produce uric acid or ammonia instead. For example, serine dehydratase converts serine to pyruvate and ammonia. After removal of one or more amino groups, the remainder of the molecule can sometimes be used to synthesize new amino acids, or it can be used for energy by entering glycolysis or the citric acid cycle, as detailed in image at right.

Complexation

Amino acids are bidentate ligands, forming transition metal amino acid complexes.

Chemical analysis

The total nitrogen content of organic matter is mainly formed by the amino groups in proteins. The Total Kjeldahl Nitrogen (TKN) is a measure of nitrogen widely used in the analysis of (waste) water, soil, food, feed and organic matter in general. As the name suggests, the Kjeldahl method is applied. More sensitive methods are available.

See also

 Amino acid dating
 Beta-peptide
 Degron
 Erepsin
 Homochirality
 Hyperaminoacidemia
 Leucines
 Miller–Urey experiment
 Nucleic acid sequence
 RNA codon table

Notes

References

Further reading

External links

Nitrogen cycle
Zwitterions

Amino acid


Isolated lung perfusion is a surgical procedure during which the circulation of blood to the lungs is separated from the circulation of blood through the rest of the body, and a drug is delivered directly into the lung circulation. This allows a higher concentration of chemotherapy to reach tumors in the lungs.

References
 Isolated lung perfusion entry in the public domain NCI Dictionary of Cancer Terms

Pulmonary thoracic surgery

Isolated lung perfusion


Walter Francis Ulmer Jr. (born April 2, 1929) is a retired lieutenant general in the United States Army.

Military career
Born in Bangor, Maine, Walter Ulmer graduated from West Point in the Class of 1952. Commissioned a second lieutenant of Armor, he commanded companies in the 56th Amphibious Tank and Tractor Battalion in Korea, the 6th Tank Battalion, 24th Infantry Division in Japan, and the 325th Airborne Infantry Regiment of the 82nd Airborne Division.   In 1958, he was assigned to the Department of Military Topography and Graphics at West Point, and, following that tour, he attended the Command and General Staff College. After graduation he deployed to Vietnam, serving with the U.S. Military Assistance Command and as senior advisor to a Vietnamese Infantry regiment. Upon his return to the United States, he held high-level staff positions and commanded the 1st Squadron, 17th Cavalry, 82nd Airborne Division from 1967 to 1968.

General Ulmer, as a Lt. Colonel, then attended the Army War College and was subsequently selected for duty on its faculty. There, at the direction of General William Westmoreland, in response to the My Lai Massacre by U.S. Army forces (and subsequent cover up by the Army chain of command), he was selected as a member of a three officer team that compiled a comprehensive and seminal study of leadership within the Army during the Vietnam War demonstrating a severe erosion of adherence to the Army's officer code of "Duty, Honor, Country".  The report, entitled 'Study on Military Professionalism', had a profound influence on Army policies, beginning with Westmoreland's decision to end the policy that officers serving in Vietnam would be rotated into a different post after only six months.

In 1972, then-Colonel Ulmer returned to Vietnam, where he was Chief, Combat Assistance Team 70, during 62 days of intense combat in the Battle and Siege of An Loc. For its extraordinary heroism against a North Vietnamese force greatly outnumbering the Army Republic of Vietnam defenders, Combat Assistance Team 70 was awarded the Presidential Unit Citation. The citation documents the team's pivotal role in turning back the North Vietnamese Army's massive surprise offensive of 1972. In 1973, General Ulmer completed a master's degree in Regional Planning from Pennsylvania State University. Subsequently, he was commander of the 194th Armor Brigade and, then, Deputy Commander, U.S. Army Armor Center, Fort Knox.  In 1975, Brigadier General Ulmer returned to West Point as the 56th Commandant of Cadets. In 1975, Ulmer served as Commandant of Cadets at the U.S. Military Academy at West Point, where he presided over the first admission of female cadets, and one of West Point's biggest embarrassments, the Class of 1977 cheating scandal involving several hundred of the junior classmen (Ulmer recommended expulsion of all cadets found guilty of cheating on an electrical engineering exam, but was overruled).

General Ulmer commanded the 3rd Armored Division in Germany and, later, during his service as Commanding General, III Corps, Fort Hood, Texas. Following promotion to lieutenant general, he commanded III Corps from 1982 to 1985  In 1985, General Ulmer retired after thirty-three years of distinguished military service. His awards and decorations include the Silver Star with Oak Leaf Cluster, the Distinguished Service Medal, the Bronze Star with Oak Leaf Cluster, the Air Medal with "V" Device, and decorations awarded by the Republic of Korea, the Republic of Vietnam, and the Federal Republic of Germany.

Awards and decorations
Lieutenant General Ulmer's awards and decorations include:
  Distinguished Service Medal
  Silver Star with one oak leaf cluster
  Bronze Star with one oak leaf cluster
  Air Medal (with Valor Device)
  Army Presidential Unit Citation
  Vietnam Service Medal
  Overseas Service Ribbon
Joint Service Commendation Medal
Army Commendation Medal with three oak leaf clusters
Legion of Merit with three oak leaf clusters

References

1929 births
Living people
Military personnel from Bangor, Maine
United States Military Academy alumni
United States Army personnel of the Vietnam War
Recipients of the Air Medal
Recipients of the Silver Star
Pennsylvania State University alumni
United States Army generals
Recipients of the Distinguished Service Medal (US Army)

Walter F. Ulmer


The Romani are an ethnic group that live in the Netherlands; part of the broader Romani diaspora. Though they represent a small portion of the national population, the plight of those in the Roma community has received ongoing national attention.

History

At the outbreak of World War II it is estimated that a number of Roma families lived in the Netherlands, forming community with a larger group of Sinti travelers and approximately 11,000 native Dutch caravan-dwellers. In 1944, toward the end of the war, Nazis in occupied Netherlands arrested 578 caravan dwellers and identified 245 as Sinti. All 245 were sent to the Auschwitz concentration camp and only 30 survived.

In 2021, King Willem-Alexander unveiled a memorial to Roma, Sinti, and Jewish victims of the Holocaust in the Netherlands.

See also
Romani diaspora

References

Romani in the Netherlands
Dutch Romani people

Romani people in the Netherlands


Jacques d'Agar (Danish: Jacob d'Agar 9 March 1640 – 16 November 1715) was a French  portrait painter born in Paris. He was a pupil of Jacob Ferdinand Voet. He began his career as an history painter, but
he soon abandoned history for portraiture, in which branch of art he became very successful.

In 1675 he was admitted into the Academy, and also became painter in ordinary to the king and his court. Upon the revocation of the Edict of Nantes, Agar, as a Protestant, was shut out from the Academy. He accordingly left France in 1682, never to return.

He was invited to the court of Denmark, and was greatly patronized by King Christian V.  His self-portrait is in the Galleria degli Uffizi in Florence, having been painted for Cosimo III de' Medici in 1693, at the request of King Christian. Walpole tells us that he visited England, where he resided some time, and met with success. He painted the portraits of several members of the British nobility of Queen Anne's reign, including the Duchess of Montagu, the Countesses of Rochfort and Sunderland, Thomas Earl of Strafford, and others. A portrait of Charles II of England, by him, is said to have been formerly in the Gallery at Christiansburg.

He died in 1716 in Copenhagen. His son Charles d'Agar also became a portrait painter.

References

Sources

Further reading

French Baroque painters
French portrait painters
1640 births
1715 deaths
Painters from Paris
Danish Baroque painters
Danish male painters
17th-century French painters
French male painters
18th-century French painters
18th-century French male artists

Jacques d'Agar


The Webb County Courthouse is located in Laredo in the U.S. state of Texas. It was added to the National Register of Historic Places in 1981.

Design
In 1907, Webb County placed ads in local newspapers announcing a contest to design a new courthouse. Famed San Antonio architect Alfred Giles submitted the winning bid on February 27, 1907. The courthouse was completed in 1909 for $46,918.

The Beaux-Arts building features a curved judge's bench. A stained glass window features "Justice" holding the scales. Tile floors are in the Mediterranean style. Alamo Iron Works produced the wrought iron staircases. Interior doors are solid wood  with brass knobs. Mansard roofed terminal pavilions feature stone-carved rams head accents. The building features yellow brick with dressings of white stone and red tile mansard roofs. The landscaping includes pecan trees and citrus trees. A cornerstone records the contractor, H. Sparbert, and architect, Alfred Giles, 1909.

Many of Alfred Giles' buildings have been demolished over the years. This fine example of his work shows why he continues to have the respect of architects, historians, and laymen alike.

In November 2010, the county held an art contest to commemorate the 100th anniversary of the courthouse. County Judge Danny Valdez and Javier Santos of the Fernando A. Salinas Charitable Trust Fund unveiled the winning design on November 12, 2010. The winning design was submitted by Jocelyn Rivera, and became a stained glass window on the third floor of the courthouse.

See also

National Register of Historic Places listings in Webb County, Texas
List of county courthouses in Texas

References

External links

Government buildings completed in 1909
Buildings and structures in Webb County, Texas
County courthouses in Texas
Courthouses on the National Register of Historic Places in Texas
National Register of Historic Places in Webb County, Texas

Webb County Courthouse (Texas)


William Robert Hamilton (–12 October 1917) was a Scottish poet and First World War soldier. He was born in Dumfries, Scotland. He emigrated to South Africa where a portion of his education was at the South African College, Cape Town. He was killed on the Western Front in Flanders, Belgium in 1917 and is remembered on the Tyne Cot Memorial, at the Tyne Cot British Cemetery and Memorial, at Ypres in Flanders, Belgium.

The reference to him reads:

Publications
 William Hamilton. Modern Poems. Oxford: B. H. Blackwell, 1917. 011648.eee.17 British Library
 William Hamilton. Moths and Fairies: A Play. 1912.

Poem by William Hamilton:

The Song of an Exile

I have seen the Cliffs of Dover
And the White Horse on the Hill;
I have walked the lanes, a rover;
I have dreamed beside the rill:
I have known the fields awaking
To the gentle touch of Spring;
The joy of morning breaking,
And the peace your twilights bring.

But I long for a sight of the pines, and the blue shadows under;For the sweet-smelling gums, and the throbbing of African air;For the sun and the sand, and the sound of the surf's ceaseless thunder,The height, and the breadth and the depth, and the nakedness there.

I have visited your cities
Where the unregenerate dwell;
I have trilled the ploughman's ditties
To the mill-wheel and the well.
I have heard the poised lark singing
To the blue of summer skies;
The whirr of pheasants winging,
And the crash when grouse arise.

But I sigh for the heat of the veld, and the cool-flowing river;For the crack of the trek-whip, the shimmer of dust-laden noon:For the day sudden dying; the croak of the frogs, and the shiverOf tropical night, and the stars, and the low-hanging moon.

I have listen'd in the gloaming
To your poets' tales of old;
I know, when I am roaming,
That I walk on hallowed mould.
I have lived and fought among you
And I trow your hearts are steel;
That the nations who deride you
Shall, like dogs, be brought to heel.

But I pine for the roar of the lion on the edge of the clearing;For the rustle of grass snake; the birds' flashing wing on the heath;For the sun-shrivelled peaks of the mountains to blue heaven rearing;The limitless outlook, the space, and the freedom beneath.

Source Original text: William Hamilton, Modern Poems (Oxford: B. H. Blackwell, 1917): 50–51. 011648.eee.17 British Library First publication date: 1917

British Army personnel of World War I
Coldstream Guards officers
20th-century Scottish poets
British military personnel killed in World War I
People from Dumfries
Scottish World War I poets
20th-century British male writers
Scottish male poets
Year of birth uncertain
1890s births

1917 deaths

William Hamilton (British Army officer)


The universal motor is a type of electric motor that can operate on either AC or DC power and uses an electromagnet as its stator to create its magnetic field. It is a commutated series-wound motor where the stator's field coils are connected in series with the rotor windings through a commutator. It is often referred to as an AC series motor. The universal motor is very similar to a DC series motor in construction, but is modified slightly to allow the motor to operate properly on AC power. This type of electric motor can operate well on AC because the current in both the field coils and the armature (and the resultant magnetic fields) will alternate (reverse polarity) synchronously with the supply. Hence the resulting mechanical force will occur in a consistent direction of rotation, independent of the direction of applied voltage, but determined by the commutator and polarity of the field coils.

Universal motors have high starting torque, can run at high speed, and are lightweight and compact. They are commonly used in portable power tools and equipment, as well as many household appliances. They're also relatively easy to control, electromechanically using tapped coils, or electronically. However, the commutator has brushes that wear, so they are much less often used for equipment that is in continuous use. In addition, partly because of the commutator, universal motors are typically very noisy, both acoustically and electromagnetically.

Working

Not all series-wound motors operate well on AC current.
If an ordinary series-wound DC motor were connected to an AC supply, it would run very poorly. The universal motor is modified in several ways to allow for proper AC supply operation. There is a compensating winding typically added, along with laminated pole pieces, as opposed to the solid pole pieces found in DC motors. A universal motor's armature typically has far more coils and plates than a DC motor, and hence fewer windings per coil. This reduces the inductance.

Efficiency
Even when used with AC power these types of motors are able to run at a rotation frequency well above that of the mains supply, and because most electric motor properties improve with speed, this means they can be lightweight and powerful. However, universal motors are usually relatively inefficient: around 30% for smaller motors and up to 70–75% for larger ones.

Torque–speed characteristics
Series-wound electric motors respond to increased load by slowing down; the current increases and the torque rises in proportion to the square of the current because the same current flows in both the armature and the field windings. If the motor is stalled, the current is limited only by the total resistance of the windings and the torque can be very high, and there is a danger of the windings becoming overheated. The counter-EMF aids the armature resistance to limit the current through the armature. When power is first applied to a motor, the armature does not rotate. At that instant, the counter-EMF is zero and the only factor limiting the armature current is the armature resistance. Usually the armature resistance of a motor is low; therefore the current through the armature would be very large when the power is applied. Therefore the need can arise for an additional resistance in series with the armature to limit the current until the motor rotation can build up the counter-EMF. As the motor rotation builds up, the resistance is gradually cut out. The speed-torque characteristic is an almost perfectly straight line between the stall torque and the no-load speed. This suits large inertial loads as the speed will drop until the motor slowly starts to rotate and these motors have a very high stalling torque.

As the speed increases, the inductance of the rotor means that the ideal commutating point changes. Small motors typically have fixed commutation. While some larger universal motors have rotatable commutation, this is rare. Instead larger universal motors often have compensation windings in series with the motor, or sometimes inductively coupled, and placed at ninety electrical degrees to the main field axis. These reduce the reactance of the armature, and improve the commutation.

One useful property of having the field windings in series with the armature winding is that as the speed increases the counter EMF naturally reduces the voltage across, and current through the field windings, giving field weakening at high speeds. This means that the motor has no theoretical maximum speed for any particular applied voltage. Universal motors can be and are generally run at high speeds, 4000–16000RPM, and can go over 20,000RPM. By way of contrast, AC synchronous and squirrel-cage induction motors cannot turn a shaft faster than allowed by the power line frequency. In countries with 60Hz AC supply, this speed is limited to 3600RPM.

Motor damage may occur from over-speeding (running at a rotational speed in excess of design limits) if the unit is operated with no significant mechanical load. On larger motors, sudden loss of load is to be avoided, and the possibility of such an occurrence is incorporated into the motor's protection and control schemes. In some smaller applications, a fan blade attached to the shaft often acts as an artificial load to limit the motor speed to a safe level, as well as a means to circulate cooling airflow over the armature and field windings. If there were no mechanical limits placed on a universal motor it could theoretically speed out of control in the same way any series-wound DC motor can.

An advantage of the universal motor is that AC supplies may be used on motors which have some characteristics more common in DC motors, specifically high starting torque and very compact design if high running speeds are used.

Disadvantages
A negative aspect is the maintenance and short life problems caused by the commutator, as well as electromagnetic interference (EMI) issues due to any sparking. Because of the relatively high maintenance commutator brushes, universal motors are best-suited for devices such as food mixers and power tools which are used only intermittently, and often have high starting-torque demands.

Another negative aspect is that these motors may only be used where mostly-clean air is present at all times. Due to the dramatically increased risk of overheating, totally-enclosed fan-cooled universal motors would be impractical, though some have been made. Such a motor would need a large fan to circulate enough air, decreasing efficiency since the motor must use more energy to cool itself. The impracticality comes from the resulting size, weight, and thermal management issues which open motors have none of.

Speed control
Continuous speed control of a universal motor running on AC is easily obtained by use of a thyristor circuit, while multiple taps on the field coil provide (imprecise) stepped speed control. Household blenders that advertise many speeds frequently combine a field coil with several taps and a diode that can be inserted in series with the motor (causing the motor to run on half-wave rectified AC).

Variations

Shunt winding
Universal motors are series wound. Shunt winding was used experimentally, in the late 19th century, but was impractical owing to problems with commutation. Various schemes of embedded resistance, inductance, and antiphase cross-coupling were attempted to reduce this. Universal motors, including shunt wound, were favoured as AC motors at this time as they were self-starting. When self-starting induction motors and automatic starters became available, these replaced the larger universal motors (above 1 hp) and the shunt wound.

Repulsion-start

In the past, repulsion-start wound-rotor motors provided high starting torque, but with added complexity. Their rotors were similar to those of universal motors, but their brushes were connected only to each other. Transformer action induced current into the rotor. Brush position relative to field poles meant that starting torque was developed by rotor repulsion from the field poles. A centrifugal mechanism, when close to running speed, connected all commutator bars together to create the equivalent of a squirrel-cage rotor. As well, when close to approximately 80 per cent of its run speed, these motors can run as induction motors.

Applications

Domestic appliances
Operating at normal power line frequencies, universal motors are not often found in a range less than . Their high speed makes them useful for appliances such as blenders, vacuum cleaners, and hair dryers where high speed and light weight are desirable. They are also commonly used in portable power tools, such as drills, sanders, circular saws, and jigsaws, where the motor's characteristics work well. An added benefit for power tools used by welders is that classic engine-driven welding machines may be a pure DC generator, and their auxiliary power receptacles will still be DC, even though a typical NEMA 5-15 household configuration. The DC power is fine for typical jobsite (outmoded) incandescent lighting and the universal motors in some drills and grinders. Many vacuum cleaner and weed trimmer motors exceed , while many Dremel and similar miniature grinders exceed .

Universal motors also lend themselves to electronic speed control and, as such, were an ideal choice for domestic washing machines. The motor can be used to agitate the drum (both forward and in reverse) by switching the field winding with respect to the armature. The motor can also be run up to the high speeds required for the spin cycle. Nowadays, variable-frequency drive motors are more commonly used instead.

Rail traction

Universal motors also formed the basis of the traditional railway traction motor in electric railways. In this application, the use of AC to power a motor originally designed to run on DC would lead to efficiency losses due to eddy current heating of their magnetic components, particularly the motor field pole-pieces that, for DC, would have used solid (un-laminated) iron. Although the heating effects are reduced by using laminated pole-pieces, as used for the cores of transformers and by the use of laminations of high-permeability electrical steel, one solution available at the start of the 20th century was for the motors to be operated from very-low-frequency AC supplies, with 25 Hz and  Hz operation being common.

Starter motor
Starters of combustion engines are usually universal motors, with the advantage of being small and having high torque at low speed. Some starters have permanent magnets, others have one of the four poles wound with a shunt coil rather than series-wound coils.

References

AC motors
Electric motors

Universal motor


Alfred Eisenack (born 13 May 1891 in Altfelde, West Prussia, died 19 April 1982 in Reutlingen) was a German paleontologist. He was a pioneer of micropaleontology and palynology. His botanical and mycological author abbreviation is "Eisenack".

Eisenack took his photographs using a Leitz monocular microscope, to which he attached a box camera fashioned from a biscuit tin and furnished with glass negatives.
He first described chitinozoans and many species of acritarchs, dinoflagellate cysts and graptolites.
In 1973 he became an honorary member of the Paleontological Society.

Biography
Eisenack went to school in Elbing and graduated in 1911 at the University of Jena and in 1913 at the University of Königsberg and began a Ph.D. thesis with Sven Tornquist about the stratigraphy of the Portlandium on Garda Lake. He was not able to finish, as his studies were interrupted by the First World War. He volunteered, and after the Battle of Łódź he was taken as a prisoner of war by the Russian army to Chita in Siberia. There he was able to improve the skills of other captive geologists (including Pontoppidan). Eisenack's return was delayed even after the Armistice. Later on he had fond memories of this time. In 1920 he worked for a time as a chemist, and returned by ship via Vladivostok to Germany.

He then studied geology with Karl Erich Andrée in Königsberg, and subsequently took a qualifying exam as a teacher. From 1925 to 1940 he worked at the Bessel High School in Königsberg, where he taught science and mathematics. He also researched microfossils from the Scandinavian Silurian and Ordovician. He began to publish papers in 1930. In 1942 he became a lecturer in Königsberg. In 1945, he was once again in Soviet captivity, in East Prussia.

After returning from Siberia in 1951, he became visiting professor at the University of Tübingen, after he had become a full-time teacher at the Oberreutlinger trade school in Reutlingen. In Tübingen, he was academically very active and also had several students. Two of his students were Hans Gocht and Gerhard Alberti - refugees from the Communist regime of East Germany; another was Karl W. Klement.

Eisenack used pre-War methods of extraction of palynomorphs from limestones. Eisenack's work extended from the Silurian  into the Ordovician  and Cambrian. Though studies of Jurassic and Oligocene palynomorphs were resumed by Eisenack (,) and work on Aptian (late Lower Cretaceous) forms initiated, his principal work thereafter was on the Palaeozoic fauna.

Dinoflagellate cyst work
Eisenack described ( ) the first Jurassic assemblages of dinoflagellate cysts to have been reported since their first brief mention by Ehrenberg. Eisenack also described assemblages from the Oligocene amber-bearing sediments of East Prussia, now Kaliningrad,
Russia, and he reported what he considered to be "hystrichospheres" from German Silurian deposits.

Acritarch work
Eisenack long resisted the use of the term Acritarch, proclaiming "die Einheitlichkeit der Hystrichospharen" - the unity of the hystrichospheres (1963a, b). In 1969 he finally conceded that he had been wrong, and adopted the name 'acritarch'.

Chitinozoans
It was Eisenack who discovered, in those same Baltic Silurian sediments, the first of the usually flask-shaped microfossils which he called chitinozoans. Eisenack considered initially that these were protozoans, perhaps related to the thecamoebians (Rhizopoda). Later he suggested an affinity to the Euglenoidea, a group of freshwater flagellated protozoans. Much later, he and others considered that these fossils were actually gastropod egg cases.

References

Dinoflagellates
Acritarchs
Palynologists
1891 births
1982 deaths
University of Königsberg alumni
University of Jena alumni
Academic staff of the University of Tübingen
German prisoners of war in World War I
World War I prisoners of war held by Russia

Alfred Eisenack


Bing Russell (May 5, 1926 - April 8, 2003) was an American actor and baseball club owner.   He was best known for playing the role of Deputy Clem Foster on Bonanza, beginning in 1959 and of Robert in The Magnificent Seven in 1960.

Russell was the father of Golden Globe nominated actor, Kurt Russell. He was also grandfather of an American actor, Wyatt Russell, who is also a former professional hockey player. Wyatt is the son of Goldie Hawn and Kurt Russell. Russell was also grandfather of a former major league baseball player, Matt Franco, who is Kurt Russell's nephew.

Early life
He was born in Brattleboro, Vermont and grew up wanting to be an actor. He studied drama at his high school. As a boy, he became an unofficial mascot of the New York Yankees, becoming friends with the players Lefty Gomez and Joe DiMaggio. Another Yankees batter, Lou Gehrig,  gave him the last bat he used to hit a home run before he retired, due to the illness ALS.

Acting career
Russell was best known for playing the role of the deputy sheriff in Bonanza along with Lorne Greene, Michael Landon, and Pernell Roberts. Bonanza was a popular cowboy television series on the NBC network that aired from 1959-1973.  He had a cowboy role in the movie The Magnificent Seven in 1960. He also guest starred in episodes of many television series during his acting career.

In 1979, Kurt Russell had the role of Elvis Presley in a television movie, Elvis and Bing Russell played his father, Vernon Presley.

Baseball
Bing Russell owned the Portland Mavericks, the only independent team in their league, from 1973 through 1977. He kept more players on his team than he needed, because he thought the players deserved to play for one last season. He believed in his players having fun. Many players who were not good enough for other teams came to his June try-outs. They were always open to anyone who showed up.

The Battered Bastards of Baseball

Archived movie film of Russell and his team became part of the 2014 documentary, The Battered Bastards of Baseball.

Kurt Russell, Russell's son, who played for the Mavericks and was vice president for the team, is in the movie.  It was directed by Chapman Way and Maclain Way, grandsons of Russell.  The movie was first shown at the Sundance Film Festival on January 20, 2014.  It began being shown on Netflix on July 11, 2014.

The Battered Bastards of Baseball got positive reviews from critics.

Scott Foundas of Variety, said that "So rife with underdog victors and hairpin twists of fortune that, if it weren't all true, no one would believe it." Duane Byrge, writing in The Hollywood Reporter, praised the movie. He said that "The Battered Bastards of Baseball is not just about baseball. It transcends the game and is a charming anti-establishment yarn that should delight audiences who don't even know an r.b.i. from a balk."

Dustin Krcatovich, from Esquire, wrote "easily one of the most raucously entertaining films to come out this year, and the best sports documentary in a while." Katie Walsh of Indiewire gave the movie a B+ grade. She said "The Batterered Bastards of Baseball is an entertaining celebration of the independent spirit and the love of the game."

The New York Daily News listed the documentary as one of the 10 best movies of 2014.

Death
Russell died from cancer on April 8, 2003 in Thousand Oaks, California.

References

Other websites

Bonanza Cast Biographies - Bing Russell

American movie actors
American television actors
Actors from Vermont
Businesspeople from Vermont
Baseball executives
1926 births
2003 deaths
Cancer deaths in California
People from Brattleboro, Vermont

Bing Russell


Craig Wright (born April 25, 1965, in San Juan, Puerto Rico) is a playwright, television producer and writer.  He is known for writing for shows including Six Feet Under and Lost and creating the television series Dirty Sexy Money and Greenleaf. He also was the screenwriter for the movie Mr. Peabody & Sherman, released March 7, 2014.

Biography
Born in 1965 in Puerto Rico, Wright attended Minnesota State University- Moorhead in Moorhead, MN, St. John's University in Collegeville, Minnesota, and went on to earn a Masters of Divinity degree from the United Theological Seminary of the Twin Cities. He lives in Los Angeles and New York City.

Playwright
Wright is known primarily for his plays: Grace, Mistakes Were Made, The Pavilion, Recent Tragic Events, Main Street and numerous others.  Wright has received awards and award nominations for his work, including the Jerome Fellowship at age 21 and apprenticeships in playwriting from the McKnight Foundation and the National Endowment for the Arts. Wright was the recipient of the 2009 Horton Foote Excellence in American Playwriting Award from Baylor University in Waco, Texas. He is a member of the ensemble of the Chicago-based A Red Orchid Theatre.

Pine City plays

Wright set four plays in Pine City, Minnesota.

Molly's Delicious, a romantic comedy, first played at the Arden Theatre Company, Philadelphia, in September 1997, directed by Aaron Posner. The play takes place in Pine City, Minnesota, in 1965.

The next play set in Pine City is Orange Flower Water, described by the Chicago Sun-Times as "a brutally honest drama about marriage and infidelity." The play premiered at Steppenwolf Theatre Company, Chicago, from October through December 2003. and ran Off-Broadway at the Edge Theater Company in April 2005.
It was published in August 2004. In 2005 it was performed at the Off-Off-Broadway Theater for the New City with a cast of Arija Bareikis, Paul Sparks, Jason Butler Harner and Pamela J. Gray, directed by Carolyn Cantor, and a 2013 production in Los Angeles was critically reviewed by Backstage.

The Pavilion premiered Off-Broadway at Rattlestick Playwrights Theater in September 2005. The Pavilion was nominated for the American Theatre Critics Association Best New Play Award and a 2005–2006 Drama Desk Award for Outstanding Play and has had over 40 productions since its premiere in 2000; in the 2008 summer season it was produced at the Westport Country Playhouse. It was also produced for Boise Contemporary Theater's 2009/10 Season.

Melissa Arctic is the last play of his Pine City works, and ran at the Folger Theatre, Washington, DC, in January and February 2004, with direction by Aaron Posner.

Other plays

Recent Tragic Events premiered at the Woolly Mammoth Theatre Company, Washington, D.C. in September 2002. The play was then produced Off-Broadway by Playwrights Horizons in September 2003. The play won an ATCA Best New Play Citation Award in 2002.

Grace premiered in October 2004 at Woolly Mammoth Theatre Company in Washington, D.C. The play premiered on Broadway at the Cort Theatre in September 2012 (previews), officially on October 4, 2012, and features Kate Arrington, Ed Asner, Paul Rudd and Michael Shannon with direction by Dexter Bullard.

His play The Unseen was performed at the Cherry Lane Theatre in New York in March 2009. Blind premiered in February 2010 at Rattlestick Playwrights Theatre in New York. The Gray Sisters premiered in April 2010 at Third Rail Rep in Portland, Oregon.

Television career
His television writing debut was on the 2001 HBO series, Six Feet Under, joining the writing staff during the 2003 season. During that season, he wrote "Twilight," for which he was nominated for an Emmy and "Timing and Space"; he penned 3 more episodes of Six Feet Under and co-wrote one with co-executive producer, Jill Soloway. In 2004, he was appointed Executive Story Editor with Nancy Oliver. In 2005, he became a producer for the fifth and final season.

In 2005, he signed a 2-year deal with Touchstone Television. He served as a supervising producer and writer for the second season of ABCs Lost in Fall 2005. He left the series midseason after co-writing two episodes. Wright and the Lost writing staff won the Writers Guild of America (WGA) Award for Best Dramatic Series at the February 2006 ceremony for their work on the first and second seasons.

Wright became a co-executive producer and writer on ABC's Brothers & Sisters in 2006.

During the 2007 season, Wright worked as the creator, head writer, and executive producer of ABC's Dirty Sexy Money, which stars Six Feet Under alumnus Peter Krause, Donald Sutherland, Samaire Armstrong and William Baldwin. The pilot was produced by Greg Berlanti and directed by Peter Horton. The series premiered in the fall of 2007.

In 2015, Wright created drama series Greenleaf for Oprah Winfrey Network.

Writing credits

Six Feet Under episodes
 Timing and Space, (2003)
 Twilight, (2003)
 Falling into Place, (2004)
 The Black Forest, with Jill Soloway, (2004)
 Time Flies, (2005)
 Static (2005)

Lost episodes
 "Orientation" (2005) with Javier Grillo-Marxuach
 "What Kate Did" (2005) with Steven Maeda

Brothers & Sisters episodes
 "Affairs of State", with Jon Robin Baitz (2006)
 "Family Portrait", with Jon Robin Baitz and Emily Whitesell (2006)
 "Mistakes Were Made, Part One", with Jon Robin Baitz (2006)

Music
A musician, Wright was co-leader of an alternative rock band The Tropicals', whose first album, Live at the Jungle, was released in 1996 . As a member of the band Kangaroo he has released three albums, Phantom, Skyscraper Spaceship and Songs (French).

References

External links

Craight Wright Internet Off-Broadway Database Listing

Living people
1965 births
20th-century American dramatists and playwrights
American soap opera writers
American television producers
Writers Guild of America Award winners
Puerto Rican dramatists and playwrights
American male screenwriters
College of Saint Benedict and Saint John's University alumni
American male television writers
American television writers
American male dramatists and playwrights
20th-century American male writers

Craig Wright (playwright)


Code 46 is a 2003 British film directed by Michael Winterbottom, written by Frank Cottrell Boyce, and starring Tim Robbins and Samantha Morton. Produced by BBC Films and Revolution Films, the film is a dystopian sci-fi love story, exploring the implications of current trends in biotechnology.

The soundtrack was composed by David Holmes and Stephen Hilton under the name "Free Association". Filmed on location in Shanghai, Dubai and Rajasthan, with interiors done onstage in London, the mesh of foreign locations was chosen due to the juxtaposition of elements in these cities offering a believable futuristic setting.

Plot
In the future, the world is divided between those who live "inside", in high-density cities, and the underclass who live "outside." Access to the cities is highly restricted and regulated through the use of health documents, known as "papeles" in the global pidgin language of the day.

William Geld, an insurance fraud investigator, is sent to Shanghai to interview employees at a company known as "The Sphinx", which manufactures the papeles. William's assignment is to identify employees who are suspected of forging "covers". After interviewing numerous Sphinx employees, he identifies a young worker named Maria Gonzalez as the forger. William is captivated by her, and instead of turning her over to security, he identifies another employee as the forger. William then meets up with Maria and they begin an affair. As Maria sleeps, William finds a forged cover in her room and takes it.

William is reprimanded for not discovering the true Sphinx forger. He requests that someone else be sent, as there may have been an accomplice to the innocent man he fingered. However, he is ordered to deal with the problem and to return to Shanghai.

Upon his return, William discovers that Maria's apartment is abandoned and the only clue is a medical clinic appointment. He visits the clinic and learns that Maria was pregnant and that the pregnancy was terminated due to a violation of Code 46. William knows that this means Maria is somehow genetically related to him, but he has no idea how.

William discovers that Maria has been taken to have her memory of the episode erased. He gets the clinic to release Maria into his care by telling them she is a witness in his fraud investigation. After she is released, William tells her about the memory erasure and about how he didn't report her for fraud. Maria is disturbed by this information and becomes very distressed. William gives her a sleeping pill and, while she is sleeping, he cuts some hair from her head and takes it to a facility providing instant DNA analysis. He discovers that Maria is a biological clone of his mother. William decides to go home to his family, but is not allowed to do so, as his 24-hour cover has expired.

William then realises that his only hope of returning home is to get a papel from Maria. She goes to work to obtain a papel, but is unable to forge one herself, as she was moved to another area of work, so a co-worker makes the cover for her. While taking a train to meet William, her memory returns and she recalls her feelings for William. He decides not to leave her.

William and Maria then travel to Jebel Ali in the UAE, which does not require special travel clearance. The two hide out in the old city where they book a room. William reveals to Maria that, in addition to the memory wiping, she has been given a virus that induces an adrenaline rush in response to physical contact with the person who brought about the Code 46 violation. He refrains from telling her the virus will also force her to report the further Code 46 violation to the authorities. They rent an old car and travel away to escape the authorities who are tracking them. William crashes the car while avoiding a collision with camels and pedestrians and they are both knocked unconscious.

William awakes in the hospital in Seattle with his wife and child. He has no memory of Maria or the Code 46 violation, as all memories of her and their time together have been replaced with memories of a successful investigation. Maria is more severely punished by being exiled "outside," to the desert. Her memories of William are altered to make them stronger, even as she is forced to live without him.

Cast

See also

List of films featuring surveillance

References

External links

 Radio interview about Code 46 with Michael Winterbottom, first broadcast on Resonance FM
 The future is now: Sci-fic in real locations

2003 films
BBC Film films
British science fiction drama films
2000s dystopian films
Films directed by Michael Winterbottom
2000s English-language films
Films about cloning
Films set in the future
2000s science fiction drama films
2003 romantic drama films
Films set in Shanghai
Films shot in Dubai
Films shot in the United Arab Emirates
Films shot in London
Films shot in Rajasthan
Films with screenplays by Frank Cottrell-Boyce
Biopunk films
Metro-Goldwyn-Mayer films
United Artists films
2003 drama films
Films scored by David Holmes (musician)
2000s British films

Code 46


Roy Levien is among the all-time most prolific inventors in the world as measured by U.S utility patents, with over 737 issued and more than 1,260 US patent applications. He is also the recipient of the Microsoft Chairman's Award from Bill Gates in 1990 for his work on applications architecture and the foundations of ActiveX. Levien co-authored the book The Keystone Advantage: What the New Dynamics of Business Ecosystems Mean for Strategy, Innovation, and Sustainability.

Levien received an M.A. in Biology from Yale University, an A.B. in Applied Mathematics from Harvard College, and has attended the doctoral programs at the Harvard Business School and Cornell's department of Neurobiology and Behavior.

References

21st-century American inventors
Harvard College alumni
Cornell University alumni
Yale University alumni
Living people
Year of birth missing (living people)

Roy Levien