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Amino Acid Code
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, 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 li ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Water
Water (chemical formula ) is an inorganic, transparent, tasteless, odorless, and nearly colorless chemical substance, which is the main constituent of Earth's hydrosphere and the fluids of all known living organisms (in which it acts as a solvent). It is vital for all known forms of life, despite not providing food, energy or organic micronutrients. Its chemical formula, H2O, indicates that each of its molecules contains one oxygen and two hydrogen atoms, connected by covalent bonds. The hydrogen atoms are attached to the oxygen atom at an angle of 104.45°. "Water" is also the name of the liquid state of H2O at standard temperature and pressure. A number of natural states of water exist. It forms precipitation in the form of rain and aerosols in the form of fog. Clouds consist of suspended droplets of water and ice, its solid state. When finely divided, crystalline ice may precipitate in the form of snow. The gaseous state of water is steam or water vapor. Water co ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Leucine
Leucine (symbol Leu or L) is an essential amino acid that is used in the biosynthesis of proteins. Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH3+ form under biological conditions), an α- carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain isobutyl group, making it a non-polar aliphatic amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Human dietary sources are foods that contain protein, such as meats, dairy products, soy products, and beans and other legumes. It is encoded by the codons UUA, UUG, CUU, CUC, CUA, and CUG. Like valine and isoleucine, leucine is a branched-chain amino acid. The primary metabolic end products of leucine metabolism are acetyl-CoA and acetoacetate; consequently, it is one of the two exclusively ketogenic amino acids, with lysine being the other. It is the most import ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycine
Glycine (symbol Gly or G; ) is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid (carbamic acid is unstable), with the chemical formula NH2‐ CH2‐ COOH. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine is integral to the formation of alpha-helices in secondary protein structure due to its compact form. For the same reason, it is the most abundant amino acid in collagen triple-helices. Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a ''Clostridium tetani'' infection) can cause spastic paralysis due to uninhibited muscle contraction. It is the only achiral proteinogenic amino acid. It can fit into hydrophilic or hydrophobic environments, due to its minimal side chain of only one hydrogen atom. History and etymology Glycine was discovered in 1820 by the French chemist He ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cysteine
Cysteine (symbol Cys or C; ) is a semiessential proteinogenic amino acid with the formula . The thiol side chain in cysteine often participates in enzymatic reactions as a nucleophile. When present as a deprotonated catalytic residue, sometimes the symbol Cyz is used. The deprotonated form can generally be described by the symbol Cym as well. The thiol is susceptible to oxidation to give the disulfide derivative cystine, which serves an important structural role in many proteins. In this case, the symbol Cyx is sometimes used. When used as a food additive, it has the E number E920. Cysteine is encoded by the codons UGU and UGC. The sulfur-containing amino acids cysteine and methionine are more easily oxidized than the other amino acids. Structure Like other amino acids (not as a residue of a protein), cysteine exists as a zwitterion. Cysteine has chirality in the older / notation based on homology to - and -glyceraldehyde. In the newer ''R''/''S'' system of designating chi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cystine
Cystine is the oxidized derivative of the amino acid cysteine and has the formula (SCH2CH(NH2)CO2H)2. It is a white solid that is poorly soluble in water. As a residue in proteins, cystine serves two functions: a site of redox reactions and a mechanical linkage that allows proteins to retain their three-dimensional structure. Formation and reactions Structure Cystine is the disulfide derived from the amino acid cysteine. The conversion can be viewed as an oxidation: : Cystine contains a disulfide bond, two amine groups, and two carboxylic acid groups. As for other amino acids, the amine and carboxylic acid groups exist is rapid equilibrium with the ammonium-carboxylate tautomer. The great majority of the literature concerns the ''l,l-''cystine, derived from ''l''-cysteine. Other isomers include ''d,d''-cystine and the meso isomer d,l-cystine, neither of which is biologically significant. Occurrence Cystine is common in many foods such as eggs, meat, dairy products, and whole ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Asparagine
Asparagine (symbol Asn or N) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain carboxamide, classifying it as a polar (at physiological pH), aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it. It is encoded by the codons AAU and AAC. History Asparagine was first isolated in 1806 in a crystalline form by French chemists Louis Nicolas Vauquelin and Pierre Jean Robiquet (then a young assistant). It was isolated from asparagus juice, in which it is abundant, hence the chosen name. It was the first amino acid to be isolated. Three years later, in 1809, Pierre Jean Robiquet identified a substance from liquorice root with properties which he qualified as very similar to those of asparagine, and which Plisson identi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Asparagus
Asparagus, or garden asparagus, folk name sparrow grass, scientific name ''Asparagus officinalis'', is a perennial flowering plant species in the genus ''Asparagus''. Its young shoots are used as a spring vegetable. It was once classified in the lily family, like the related ''Allium'' species, onions and garlic. However, genetic research places lilies, ''Allium'', and asparagus in three separate families—the Liliaceae, Amaryllidaceae, and Asparagaceae, respectively— the Amaryllidaceae and Asparagaceae are grouped together in the order Asparagales. Sources differ as to the native range of ''Asparagus officinalis'', but generally include most of Europe and western temperate Asia. It is widely cultivated as a vegetable crop. Description Asparagus is a herbaceous, perennial plant growing to tall, with stout stems with much-branched, feathery foliage. The 'leaves' are in fact needle-like cladodes ( modified stems) in the axils of scale leaves; they are long and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pierre Jean Robiquet
Pierre Jean Robiquet (13 January 1780 – 29 April 1840) was a French chemist. He laid founding work in identifying amino acids, the fundamental building blocks of proteins. He did this through recognizing the first of them, asparagine, in 1806, in the industry's adoption of industrial dyes, with the identification of alizarin in 1826, and in the emergence of modern medications, through the identification of codeine in 1832, a opiate alkaloid substance of widespread use with analgesic and antidiarrheal properties. Robiquet was born in Rennes. He was at first a pharmacist in the French armies during the French Revolution years and became a professor at the École de pharmacie in Paris, where he died. Notable scientific achievements were among other things his isolation and characterization of properties of asparagine (the first amino acid to be identified, from asparagus, achieved. In 1806, with Louis Nicolas Vauquelin), cantharidin (1810), the sigma-1 receptor agonist noscapi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Louis-Nicolas Vauquelin
Prof. Louis Nicolas Vauquelin FRS(For) HFRSE (16 May 1763 – 14 November 1829) was a French pharmacist and chemist. He was the discoverer of both chromium and beryllium. Early life Vauquelin was born at Saint-André-d'Hébertot in Normandy, France, the son of Nicolas Vauquelin, an estate manager, and his wife, Catherine Le Charterier. His first acquaintance with chemistry was gained as laboratory assistant to an apothecary in Rouen (1777–1779), and after various vicissitudes he obtained an introduction to A. F. Fourcroy, in whose laboratory he was an assistant from 1783 to 1791. Moving to Paris, he became a laboratory assistant at the Jardin du Roi and was befriended by a professor of chemistry. In 1791 he was made a member of the Academy of Sciences and from that time he helped to edit the journal ''Annales de Chimie'' ''(Chemical annals)'', although he left the country for a while during the height of the French Revolution. In 1798 Vauquelin discovered beryllium oxide by ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Abiogenesis
In biology, abiogenesis (from a- 'not' + Greek bios 'life' + genesis 'origin') or the origin of life is the natural process by which life has arisen from non-living matter, such as simple organic compounds. The prevailing scientific hypothesis is that the transition from non-living to living entities on Earth was not a single event, but an evolutionary process of increasing complexity that involved the formation of a habitable planet, the prebiotic synthesis of organic molecules, molecular self-replication, self-assembly, autocatalysis, and the emergence of cell membranes. Many proposals have been made for different stages of the process. The study of abiogenesis aims to determine how pre-life chemical reactions gave rise to life under conditions strikingly different from those on Earth today. It primarily uses tools from biology and chemistry, with more recent approaches attempting a synthesis of many sciences. Life functions through the specialized chemistry of carbon and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biosynthesis
Biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism. The prerequisite elements for biosynthesis include: precursor compounds, chemical energy (e.g. ATP), and catalytic enzymes which may require coenzymes (e.g.NADH, NADPH). These elements create monomers, the building blocks for macromolecules. Some important biological macromolecules include: proteins, which are composed of amino acid monomers joined via peptide bon ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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