Proline is a proteinogenic amino acid, used in the biosynthesis of proteins. It contains an α-amino group, an α-carboxylic acid group, a side chain pyrrolidine, classifying it as a nonpolar, aliphatic amino acid, it is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting with CC. Proline is the only proteinogenic amino acid with a secondary amine, in that the alpha-amino group is attached directly to the main chain, making the α carbon a direct substituent of the side chain. Proline was first isolated in 1900 by Richard Willstätter who obtained the amino acid while studying N-methylproline; the year after Emil Fischer published the synthesis of proline from phthalimide propylmalonic ester. The name proline comes from one of its constituents. Proline is biosynthetically derived from the amino acid L-glutamate. Glutamate-5-semialdehyde is first formed by glutamate 5-kinase and glutamate-5-semialdehyde dehydrogenase.

This can either spontaneously cyclize to form 1-pyrroline-5-carboxylic acid, reduced to proline by pyrroline-5-carboxylate reductase, or turned into ornithine by ornithine aminotransferase, followed by cyclisation by ornithine cyclodeaminase to form proline. L-Proline has been found to act as a weak agonist of the glycine receptor and of both NMDA and non-NMDA ionotropic glutamate receptors, it has been proposed to be a potential endogenous excitotoxin. In plants, proline accumulation is a common physiological response to various stresses but is part of the developmental program in generative tissues; the distinctive cyclic structure of proline's side chain gives proline an exceptional conformational rigidity compared to other amino acids. It affects the rate of peptide bond formation between proline and other amino acids; when proline is bound as an amide in a peptide bond, its nitrogen is not bound to any hydrogen, meaning it cannot act as a hydrogen bond donor, but can be a hydrogen bond acceptor.

Peptide bond formation with incoming Pro-tRNAPro is slower than with any other tRNAs, a general feature of N-alkylamino acids. Peptide bond formation is slow between an incoming tRNA and a chain ending in proline; the exceptional conformational rigidity of proline affects the secondary structure of proteins near a proline residue and may account for proline's higher prevalence in the proteins of thermophilic organisms. Protein secondary structure can be described in terms of the dihedral angles φ, ψ and ω of the protein backbone; the cyclic structure of proline's side chain locks the angle φ at −65°. Proline acts as a structural disruptor in the middle of regular secondary structure elements such as alpha helices and beta sheets. Proline is commonly found in turns, aids in the formation of beta turns; this may account for the curious fact that proline is solvent-exposed, despite having a aliphatic side chain. Multiple prolines and/or hydroxyprolines in a row can create a polyproline helix, the predominant secondary structure in collagen.

The hydroxylation of proline by prolyl hydroxylase increases the conformational stability of collagen significantly. Hence, the hydroxylation of proline is a critical biochemical process for maintaining the connective tissue of higher organisms. Severe diseases such as scurvy can result from defects in this hydroxylation, e.g. mutations in the enzyme prolyl hydroxylase or lack of the necessary ascorbate cofactor. Peptide bonds to proline, to other N-substituted amino acids, are able to populate both the cis and trans isomers. Most peptide bonds overwhelmingly adopt the trans isomer, chiefly because the amide hydrogen offers less steric repulsion to the preceding Cα atom than does the following Cα atom. By contrast, the cis and trans isomers of the X-Pro peptide bond both experience steric clashes with the neighboring substitution and have a much lower energy difference. Hence, the fraction of X-Pro peptide bonds in the cis isomer under unstrained conditions is elevated, with cis fractions in the range of 3-10%.

However, these values depend on the preceding amino acid, with Gly and aromatic residues yielding increased fractions of the cis isomer. Cis fractions up to 40% have been identified for Aromatic-Pro peptide bonds. From a kinetic standpoint, cis-trans proline isomerization is a slow process that can impede the progress of protein folding by trapping one or more proline residues crucial for folding in the non-native isomer when the native protein requires the cis isomer; this is because proline residues are synthesized in the ribosome as the trans isomer form. All organisms possess prolyl isomerase enzymes to catalyze this isomerization, some bacteria have specialized prolyl isomerases associated with the ribosome. However, not all prolines are essential for folding, protein folding may proceed at a normal rate despite having non-native conformers of many X-Pro peptide bonds. Proline and its derivatives are used as asymmetric catalys

List of gates in India Northbrook Gate Sabhyata Dwar Ajmeri Gate Alai Darwaza Bahadur Shahi Gate Delhi Gate Delhi Gate Entrance to Humayun's Tomb Entrance to Jama Masjid Entrance of the Mausoleum of Ghiyath al-Din Tughluq at Tughlaqabad Fort Gateway into Arab Sarai, near Humayun's Tomb Complex India Gate Jamali Kamali Entrance, Mehrauli Kabuli Gate Kashmiri Gate Khooni Darwaza Lahori Gate Lal Darwaza Main Gate to Tomb of Safdarjung Nigambodh Gate Tripolia Gates Turkman Gate Water Gate of Red Fort Zafar Gate of Zafar Mahal, Mehrauli Akshardwar, Shri Swaminarayan Mandir, Bhavnagar Gates of Ahmedabad Sayajirao Palace Gate, Vadodara Tan Darvajaa, Dhoraji Teen Darwaza, Bhadra Fort, Ahmedabad Ray Gate, Junagadh Majhevdi Gate, Junagadh. Bidar Fort Gate, Bidar Daria Daulat Bagh Gate, Srirangapatna Vittala Temple Gate, Hampi Alamgir Darwaza, Mandu Badalgarh Gate at Gwalior Fort Bhopal Gate, Bhopal Entrance Gate of Taj-ul-Masajid, Bhopal Entrance to Moti Masjid, Bhopal Gadi Darwaza, Mandu Gate of Teli Mandir Gwalior Hathi Pol at Gwalior Fort Sanchi Gateways, Sanchi Ratlami Gate, Jaora Bhadkal Gate, Aurangabad Delhi Gate, Aurangabad Entrance to Bibi Ka Maqbara,Aurangabad Gateway of aurangabad, aurangabad Kaala Gate, Aurangabad Mahmood Gate, Aurangabad Makai Gate, Aurangabad Mecca Gate, Aurangabad Paithan Gate, Aurangabad Rangeen Gate, Aurangabad Roshan Gate, Aurangabad Katkat Gate, Aurangabad Barapulla Gate, Aurangabad Naubat Gate, Aurangabad Khaas Gate, Aurangabad Jaffar Gate, Aurangabad Begum Gate, Aurangabad Chota Bhadkal Gate, Aurangabad Hathi Gate, Aurangabad Khooni Gate, Aurangabad Mir Adil Gate, Aurangabad Buland Gate, Aurangabad Nurmahal Sarai Mughal Gateway Chandpole, Chanpori Gate, Ajmeri gate, New gate, Sanganeri gate, Ghat gate, Samrat gate, Zorawar Singh Gate at Jaipur Ganesh Pol, Suraj Pol, Tripolia gate, Lion gate at Amer Fort, Jaipur Hanuman Pol at Kumbhalgarh, Rajsamand District Jayapol, Dedh Kamgra Pol and Loha Pol at Mehrangarh Fort in Jodhpur Karan Pol, Suraj Pol, Daulat Pol, Chand Pol and Fateh Pol at Junagarh Fort, Bikaner Ram Pol, Padan Pol, Bhairon Pol, Hanuman Pol, Ganesh Pol, Jodla Pol, Laxman Pol at Chittor Fort Chowmahalla Palace gate tower, Hyderabad Kakatiya Kala Thoranam or Warangal Gate Babe Syed Gate, Aligarh Muslim University, Aligarh Amar Singh Gate, Agra Buland Darwaza, Fatehpur Sikri Entrance Gate to Jama Masjid, Agra Entrance Gate to Tomb of Akbar the Great, Agra Entrance Gate to Tomb of I'timād-ud-Daulah, Agra Entrance to Bahu Begum ka Maqbara, Faizabad Gateway to Bara Imambara, Lucknow Gateway to Gulab Bari, Faizabad Great gate Taj Mahal, Agra Laal Darwaza, Ramnagar Fort, Varanasi Rumi Darwaza, Lucknow Shahji Temple Gate, Vrindavan Fort and Gates of Ahmedabad Gates in Aurangabad, Maharashtra Gates of Delhi

Steward Observatory is the research arm of the Department of Astronomy at the University of Arizona. Its offices are located on the UA campus in Arizona. Established in 1916, the first telescope and building were formally dedicated on April 23, 1923, it now operates, or is a partner in telescopes at five mountain-top locations in Arizona, one in New Mexico, one in Hawaii, one in Chile. It has provided instruments for numerous terrestrial ones. Steward has one of the few facilities in the world that can cast and figure the large primary mirrors used in telescopes built in the early 21st century. Steward Observatory owes its existence to the efforts of American astronomer and dendrochronologist Andrew Ellicott Douglass. In 1906, Douglass accepted a position as Assistant Professor of Physics and Geography at the University of Arizona in Tucson, Arizona. Upon his arrival in Tucson, Douglass established astronomical research programs using an 8-inch refracting telescope on loan from the Harvard College Observatory and began to pursue funding to construct a large research-class telescope in Tucson.

Over the next 10 years, all of Douglass’ efforts to secure funding from the University and the Arizona Territorial Legislatures ended in failure. During this time period, Douglass served the University of Arizona as Head of the Dept. of Physics and Astronomy, Interim President, Dean of the College of Letters, Arts, & Sciences. On October 18, 1916, University President Rufus von KleinSmid announced that an anonymous donor had given the University $60,000 “…to be used to buy a telescope of huge size.” That donor was revealed to be Mrs. Lavinia Steward of Oracle, Arizona. Mrs. Steward was a wealthy widow who had an interest in astronomy and a desire to memorialize her late husband, Mr. Henry Steward. Douglass made plans to use the Steward gift to construct a 36-inch diameter Newtonian reflecting telescope; the Warner & Swasey Company of Cleveland, Ohio was contracted to build the telescope, but the United States entry into World War I delayed the contract since Warner & Swasey had war contracts that took priority.

The situation was further delayed by the fact that up until this time, the expertise in large telescope mirror making was in Europe. The war made it impossible to contract with a European company. So Douglass had to find an American glass company, willing to develop this expertise. After a couple of failed castings, the Spencer Lens Co. of Buffalo, New York produced a 36-inch mirror for the Steward Telescope. The telescope was installed in the observatory building in July 1922, the Steward Observatory was dedicated on April 23, 1923. In his dedication address, Douglass recounted the trials and tribulations of establishing the observatory gave the following eloquent justification for the scientific endeavor: In concluding I wish to leave with you a more general view; this installation is to be devoted to scientific research. Scientific research is business foresight on a large scale, it is knowledge obtained. Knowledge is power, but we cannot tell which fact in the domain of knowledge is the one, going to give the power, we therefore develop the idea of knowledge for its own sake, confident that some one fact or training will pay for all the effort.

This I believe is the essence of education wherever such education is not vocational. The student has much training, he can only dimly see which fact and which training will be of eminent use to him, but some special part of his education will take root in him and grow and pay for all of the effort which he and his friends have put into it. So it is with the research institutions. In this Observatory I sincerely hope and expect that the boundaries of human knowledge will be advanced along astronomical lines. Astronomy was the first science developed by our primitive ancestors thousands of years ago because it measured time. Performing that same function, it has played a vast part in human history, today it is telling us facts, forever wonderful, about the size of our universe. Steward Observatory manages three different observing locations in southern Arizona: Mount Graham International Observatory, Mount Lemmon Observatory, Catalina Station on Mount Bigelow, it operates telescopes at two additional important observatories: Kitt Peak National Observatory and Fred Lawrence Whipple Observatory on Mount Hopkins.

Steward is a partner in the Sloan Digital Sky Survey-III, located in New Mexico at Apache Point Observatory. Steward maintains a student observatory on Tumamoc Hill 5 kilometers west of the campus; the original observatory building in Tucson is used only for public outreach and undergraduate general education. The Arizona Radio Observatory, a subsidiary of Steward Observatory, operates one telescope each at KPNO and MGIO. Steward Observatory participates in three international projects, it is a full member in the twin Magellan Telescopes at Las Campanas Observatory in northern Chile. It is a member in two projects planned for same region: the Large Synoptic Survey Telescope and the Giant Magellan Telescope, a next generation large telescope; the Richard F. Caris Mirror Laboratory is fabricating and finishing the mirrors for both telescopes, made the two Magellan mirrors; the Richard F. Caris Mirror Laboratory, located under the east side of Arizona Stadium, has pioneered new techniques of large mirror production, including spin-casting lightweight honeycomb mirrors in a rotating furnace

Canaiolo is a red Italian wine grape grown through Central Italy but is most noted in Tuscany. Other regions with plantings of Canaiolo include Lazio and Sardegna. In Umbria a white berried mutation known as Canaiolo bianco exists. Together with Sangiovese and Colorino it is used to create Chianti wine and is an important but secondary component of Vino Nobile di Montepulciano. In the history of Chianti it has been a key component blend and during the 18th century may have been the grape used in higher percentage than Sangiovese. Part of its popularity may have been the grape's ability to dry out without rotting for use in the governo method of prolonging fermentation. In the 19th century, the Chianti recipe of Bettino Ricasoli called for Canaiolo to play a supporting role to Sangiovese, adding fruitiness and softening tannins without detracting from the wine's aromas. In the aftermath of the phylloxera epidemic, the Canaiolo vines did not take well to grafting onto new American rootstock and the grape began to fall out of favor.

As of 2006, total plantings of Canaiolo throughout Italy dropped to under 7,410 acres. Today there are renewed efforts by Tuscan winemakers to find better clonal selections and re-introduce the variety into popular usage. A white sub-variety exists, known as Canaiolo bianco, a permitted grape variety in the Umbrian wine region of Orvieto where is known as Drupeggio. In recent years plantings have been declining. Ampelographers believe that Canaiolo is most native to Central Italy and to the Tuscany region, it was a planted variety in the Chianti region and most was the dominant grape variety in Chianti blends throughout the 18th century. The writings of Italian writer Cosimo Villifranchi noted the grape's popularity and that it was blended with Sangiovese and Marzemino. Part of Canaiolo's success in the region may have been its affinity for the governo winemaking technique, used to ensure complete fermentation. At the time various wine faults would plague unstable Chiantis because they were not able to complete fermentation and yeast cells would remain active in the wine.

The lack of full fermentation was due to cooler temperatures following harvest that stuns the yeast and prohibits activity prior to technological advances in temperature control fermentation vessel. The technique of governo was first developed by Chianti winemakers in the 14th century; this involves adding half-dried grapes to the must to stimulate the yeast with a fresh source of sugar that may keep the yeast active all the through the fermentation process. Canaiolo's resistance to rotting while going through the partial drying process made it an ideal grape for this technique. In the 19th century, the Baron Bettino Ricasoli created the modern Chianti recipe, predominantly Sangiovese with Canaiolo added for it fruitiness and ability to soften the tannins of Sangiovese. Wine expert Hugh Johnson has noted that the relationship between Sangiovese and Canaiolo has some parallels to how Cabernet Sauvignon is softened by the fruit of Merlot in the traditional Bordeaux style blend; the rise in prominence of Sangiovese herald the decline of Canaiolo as more winemakers rushed to plant more Sangiovese.

Outside of Chianti, Canaiolo role in the Sangiovese based on Vino Nobile di Montepulciano was declining though it was never as prominent as it once was in Chianti. The phylloxera devastation at the end of the 19th century highlighted the unique difficulties that Canaiolo has with grafting as many plantings on new American rootstock failed to take. Today there are a few vineyards in the Chianti Classico region specializing in Canaiolo, two of them being the family estates of Bettino Ricasoli in Brolio and Gaiole in Chianti as well as a scattering of vineyards in Barberino Val d'Elsa. There are renewed efforts and research in clonal selections to revive the variety in Tuscany. Outside of Tuscany, Canaiolo is found throughout central Italy with significant plantings in Lazio and Sardegna. Though there are efforts in Tuscany to revive the variety, plantings throughout the country continue to drop and fell under 7,410 acres in 2006. Canaiolo is known under the synonyms Caccione nero, Cacciuna nera, Calabrese, Canaiolo Borghese, Canaiolo Cascolo, Canaiolo Colore, Canaiolo Grosso, Canaiolo nero, Canaiolo nero a Raspo rosso, Canaiolo nero Comune, Canaiolo nero Grosso, Canaiolo nero Minuto, Canaiolo Pratese, Canaiolo Romano, Canaiolo rosso Piccolo, Canaiolo Toscano, Canaiuolo, Canajola Lastri, Canajolo Lastri, Canajolo nero Grosso, Canajolo Piccolo, Canajuolo nero Comune, Cannaiola, Colore, San Giovese, Tindilloro, Uva Canaiolo, Uva Canajuola, Uva Canina, Uva Colore Canaiola, Uva Dei Cani, Uva Donna, Uva Fosca, Uva Grossa, Uva Marchigiana, Uva Merla, Vitis Vinifera Etrusca.

Chianti Producers Association

The 2002 Africa Cup of Nations was the 23rd edition of the Africa Cup of Nations, the association football championship of Africa. It was hosted by Mali. Just like in 2000, the field of sixteen teams was split into four groups of four. Cameroon won its fourth championship. Bids: Algeria Botswana Egypt Ethiopia MaliThe organization of the 2002 Africa Cup of Nations was awarded to Mali on 5 February 1998 by the CAF Executive Committee meeting in Ouagadougou, Burkina Faso during the 1998 African Cup of Nations. Voters had a choice between five countries: Algeria, Egypt and Mali; this was the first time. Teams highlighted in green progress to the Quarter Finals. 3 goals 2 goals 1 goal Goalkeeper Tony SylvaDefenders Taribo West Rigobert Song Ifeanyi Udeze Hany RamzyMidfielders Seydou Keita Rafik Saifi Patrick M'Boma Sibusiso ZumaForwards Julius Aghahowa El Hadji Diouf Details at RSSSF

Evdokia Kadi is a Cypriot singer who represented Cyprus at the Eurovision Song Contest 2008, with the song "Femme Fatale". She was eliminated in the second semi-final on May 22 and therefore did not make it to the final, she started her singing career in 2001 at the University of Cyprus. Since she has taken part in many concerts in Cyprus and abroad alongside several Greek and Cypriot singers and performers, she is a member of the CyBC orchestra. Following her performance at Eurovision, Kadi went to Greece in August where she performed with Nikos Kourkoulis at Poseidon nightclub, she was planning to release her debut album in December 2008. Cyprus in the Eurovision Song Contest 2008