Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, transporting molecules from one location to another. Proteins differ from one another in their sequence of amino acids, dictated by the nucleotide sequence of their genes, which results in protein folding into a specific three-dimensional structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are considered to be proteins and are called peptides, or sometimes oligopeptides; the individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, encoded in the genetic code.
In general, the genetic code specifies 20 standard amino acids. Shortly after or during synthesis, the residues in a protein are chemically modified by post-translational modification, which alters the physical and chemical properties, stability and the function of the proteins. Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can work together to achieve a particular function, they associate to form stable protein complexes. Once formed, proteins only exist for a certain period and are degraded and recycled by the cell's machinery through the process of protein turnover. A protein's lifespan covers a wide range, they can exist for years with an average lifespan of 1 -- 2 days in mammalian cells. Abnormal or misfolded proteins are degraded more either due to being targeted for destruction or due to being unstable. Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms and participate in every process within cells.
Many proteins are enzymes that are vital to metabolism. Proteins have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell signaling, immune responses, cell adhesion, the cell cycle. In animals, proteins are needed in the diet to provide the essential amino acids that cannot be synthesized. Digestion breaks the proteins down for use in the metabolism. Proteins may be purified from other cellular components using a variety of techniques such as ultracentrifugation, precipitation and chromatography. Methods used to study protein structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance and mass spectrometry. Most proteins consist of linear polymers built from series of up to 20 different L-α- amino acids. All proteinogenic amino acids possess common structural features, including an α-carbon to which an amino group, a carboxyl group, a variable side chain are bonded.
Only proline differs from this basic structure as it contains an unusual ring to the N-end amine group, which forces the CO–NH amide moiety into a fixed conformation. The side chains of the standard amino acids, detailed in the list of standard amino acids, have a great variety of chemical structures and properties; the amino acids in a polypeptide chain are linked by peptide bonds. Once linked in the protein chain, an individual amino acid is called a residue, the linked series of carbon and oxygen atoms are known as the main chain or protein backbone; the peptide bond has two resonance forms that contribute some double-bond character and inhibit rotation around its axis, so that the alpha carbons are coplanar. The other two dihedral angles in the peptide bond determine the local shape assumed by the protein backbone; the end with a free amino group is known as the N-terminus or amino terminus, whereas the end of the protein with a free carboxyl group is known as the C-terminus or carboxy terminus.
The words protein and peptide are a little ambiguous and can overlap in meaning. Protein is used to refer to the complete biological molecule in a stable conformation, whereas peptide is reserved for a short amino acid oligomers lacking a stable three-dimensional structure. However, the boundary between the two is not well defined and lies near 20–30 residues. Polypeptide can refer to any single linear chain of amino acids regardless of length, but implies an absence of a defined conformation. Proteins can interact with many types of molecules, including with other proteins, with lipids, with carboyhydrates, with DNA, it has been estimated. Smaller bacteria, such as Mycoplasma or spirochetes contain fewer molecules, on the order of 50,000 to 1 million. By contrast, eukaryotic cells are larger and thus contain much more pro
International Standard Serial Number
An International Standard Serial Number is an eight-digit serial number used to uniquely identify a serial publication, such as a magazine. The ISSN is helpful in distinguishing between serials with the same title. ISSN are used in ordering, interlibrary loans, other practices in connection with serial literature; the ISSN system was first drafted as an International Organization for Standardization international standard in 1971 and published as ISO 3297 in 1975. ISO subcommittee TC 46/SC 9 is responsible for maintaining the standard; when a serial with the same content is published in more than one media type, a different ISSN is assigned to each media type. For example, many serials are published both in electronic media; the ISSN system refers to these types as electronic ISSN, respectively. Conversely, as defined in ISO 3297:2007, every serial in the ISSN system is assigned a linking ISSN the same as the ISSN assigned to the serial in its first published medium, which links together all ISSNs assigned to the serial in every medium.
The format of the ISSN is an eight digit code, divided by a hyphen into two four-digit numbers. As an integer number, it can be represented by the first seven digits; the last code digit, which may be 0-9 or an X, is a check digit. Formally, the general form of the ISSN code can be expressed as follows: NNNN-NNNC where N is in the set, a digit character, C is in; the ISSN of the journal Hearing Research, for example, is 0378-5955, where the final 5 is the check digit, C=5. To calculate the check digit, the following algorithm may be used: Calculate the sum of the first seven digits of the ISSN multiplied by its position in the number, counting from the right—that is, 8, 7, 6, 5, 4, 3, 2, respectively: 0 ⋅ 8 + 3 ⋅ 7 + 7 ⋅ 6 + 8 ⋅ 5 + 5 ⋅ 4 + 9 ⋅ 3 + 5 ⋅ 2 = 0 + 21 + 42 + 40 + 20 + 27 + 10 = 160 The modulus 11 of this sum is calculated. For calculations, an upper case X in the check digit position indicates a check digit of 10. To confirm the check digit, calculate the sum of all eight digits of the ISSN multiplied by its position in the number, counting from the right.
The modulus 11 of the sum must be 0. There is an online ISSN checker. ISSN codes are assigned by a network of ISSN National Centres located at national libraries and coordinated by the ISSN International Centre based in Paris; the International Centre is an intergovernmental organization created in 1974 through an agreement between UNESCO and the French government. The International Centre maintains a database of all ISSNs assigned worldwide, the ISDS Register otherwise known as the ISSN Register. At the end of 2016, the ISSN Register contained records for 1,943,572 items. ISSN and ISBN codes are similar in concept. An ISBN might be assigned for particular issues of a serial, in addition to the ISSN code for the serial as a whole. An ISSN, unlike the ISBN code, is an anonymous identifier associated with a serial title, containing no information as to the publisher or its location. For this reason a new ISSN is assigned to a serial each time it undergoes a major title change. Since the ISSN applies to an entire serial a new identifier, the Serial Item and Contribution Identifier, was built on top of it to allow references to specific volumes, articles, or other identifiable components.
Separate ISSNs are needed for serials in different media. Thus, the print and electronic media versions of a serial need separate ISSNs. A CD-ROM version and a web version of a serial require different ISSNs since two different media are involved. However, the same ISSN can be used for different file formats of the same online serial; this "media-oriented identification" of serials made sense in the 1970s. In the 1990s and onward, with personal computers, better screens, the Web, it makes sense to consider only content, independent of media; this "content-oriented identification" of serials was a repressed demand during a decade, but no ISSN update or initiative occurred. A natural extension for ISSN, the unique-identification of the articles in the serials, was the main demand application. An alternative serials' contents model arrived with the indecs Content Model and its application, the digital object identifier, as ISSN-independent initiative, consolidated in the 2000s. Only in 2007, ISSN-L was defined in the
In cell biology, the cytoplasm is all of the material within a cell, enclosed by the cell membrane, except for the cell nucleus. The material inside the nucleus and contained within the nuclear membrane is termed the nucleoplasm; the main components of the cytoplasm are cytosol – a gel-like substance, the organelles – the cell's internal sub-structures, various cytoplasmic inclusions. The cytoplasm is about 80% water and colorless; the submicroscopic ground cell substance, or cytoplasmatic matrix which remains after exclusion the cell organelles and particles is groundplasm. It is the hyaloplasm of light microscopy, high complex, polyphasic system in which all of resolvable cytoplasmic elements of are suspended, including the larger organelles such as the ribosomes, the plant plastids, lipid droplets, vacuoles. Most cellular activities take place within the cytoplasm, such as many metabolic pathways including glycolysis, processes such as cell division; the concentrated inner area is called the endoplasm and the outer layer is called the cell cortex or the ectoplasm.
Movement of calcium ions in and out of the cytoplasm is a signaling activity for metabolic processes. In plants, movement of the cytoplasm around vacuoles is known as cytoplasmic streaming; the term was introduced by Rudolf von Kölliker in 1863 as a synonym for protoplasm, but it has come to mean the cell substance and organelles outside the nucleus. There has been certain disagreement on the definition of cytoplasm, as some authors prefer to exclude from it some organelles the vacuoles and sometimes the plastids; the physical properties of the cytoplasm have been contested in recent years. It remains uncertain how the varied components of the cytoplasm interact to allow movement of particles and organelles while maintaining the cell’s structure; the flow of cytoplasmic components plays an important role in many cellular functions which are dependent on the permeability of the cytoplasm. An example of such function is cell signalling, a process, dependent on the manner in which signaling molecules are allowed to diffuse across the cell.
While small signaling molecules like calcium ions are able to diffuse with ease, larger molecules and subcellular structures require aid in moving through the cytoplasm. The irregular dynamics of such particles have given rise to various theories on the nature of the cytoplasm. There has long been evidence, it is thought that the component molecules and structures of the cytoplasm behave at times like a disordered colloidal solution and at other times like an integrated network, forming a solid mass. This theory thus proposes that the cytoplasm exists in distinct fluid and solid phases depending on the level of interaction between cytoplasmic components, which may explain the differential dynamics of different particles observed moving through the cytoplasm, it has been proposed that the cytoplasm behaves like a glass-forming liquid approaching the glass transition. In this theory, the greater the concentration of cytoplasmic components, the less the cytoplasm behaves like a liquid and the more it behaves as a solid glass, freezing larger cytoplasmic components in place.
A cell's ability to vitrify in the absence of metabolic activity, as in dormant periods, may be beneficial as a defence strategy. A solid glass cytoplasm would freeze subcellular structures in place, preventing damage, while allowing the transmission of small proteins and metabolites, helping to kickstart growth upon the cell's revival from dormancy. There has been research examining the motion of cytoplasmic particles independent of the nature of the cytoplasm. In such an alternative approach, the aggregate random forces within the cell caused by motor proteins explain the non-Brownian motion of cytoplasmic constituents; the three major elements of the cytoplasm are the cytosol and inclusions. The cytosol is the portion of the cytoplasm not contained within membrane-bound organelles. Cytosol makes up about 70% of the cell volume and is a complex mixture of cytoskeleton filaments, dissolved molecules, water; the cytosol's filaments include the protein filaments such as actin filaments and microtubules that make up the cytoskeleton, as well as soluble proteins and small structures such as ribosomes and the mysterious vault complexes.
The inner and more fluid portion of the cytoplasm is referred to as endoplasm. Due to this network of fibres and high concentrations of dissolved macromolecules, such as proteins, an effect called macromolecular crowding occurs and the cytosol does not act as an ideal solution; this crowding effect alters. Organelles, are membrane-bound structures inside the cell that have specific functions; some major organelles that are suspended in the cytosol are the mitochondria, the endoplasmic reticulum, the Golgi apparatus, lysosomes, in plant cells, chloroplasts. The inclusions are small particles of insoluble substances suspended in the cytosol. A huge range of inclusions exist in different cell types, range from crystals of calcium oxalate or silicon dioxide in plants, to granules of energy-storage materials such as starch, glycogen, or polyhydroxybutyrate. A widespread example are lipid droplets, which are spherical droplets composed of lipids and proteins that are used in both prokaryotes and eukaryotes as a way of storing lipids such as fatty acids and sterols.
Lipid droplets make up much of the volume of adipocytes, which are specialized lipid-st
G proteins known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, are involved in transmitting signals from a variety of stimuli outside a cell to its interior. Their activity is regulated by factors that control their ability to bind to and hydrolyze guanosine triphosphate to guanosine diphosphate; when they are bound to GTP, they are'on', when they are bound to GDP, they are'off'. G proteins belong to the larger group of enzymes called GTPases. There are two classes of G proteins; the first function as monomeric small GTPases, while the second function as heterotrimeric G protein complexes. The latter class of complexes is made up of alpha and gamma subunits. In addition, the beta and gamma subunits can form a stable dimeric complex referred to as the beta-gamma complex. Heterotrimeric G proteins located within the cell are activated by G protein-coupled receptors that span the cell membrane. Signaling molecules bind to a domain of the GPCR located outside the cell, an intracellular GPCR domain in turn activates a particular G protein.
Some inactive-state GPCRs have been shown to be "pre-coupled" with G proteins. The G protein activates a cascade of further signaling events that results in a change in cell function. G protein-coupled receptor and G proteins working together transmit signals from many hormones, neurotransmitters, other signaling factors. G proteins regulate metabolic enzymes, ion channels, transporter proteins, other parts of the cell machinery, controlling transcription, motility and secretion, which in turn regulate diverse systemic functions such as embryonic development and memory, homeostasis. G proteins were discovered when Alfred G. Gilman and Martin Rodbell investigated stimulation of cells by adrenaline, they found that when adrenaline binds to a receptor, the receptor does not stimulate enzymes directly. Instead, the receptor stimulates a G protein, which stimulates an enzyme. An example is adenylate cyclase, which produces the second messenger cyclic AMP. For this discovery, they won the 1994 Nobel Prize in Medicine.
Nobel prizes have been awarded for many aspects of signaling by G GPCRs. These include receptor antagonists, neurotransmitters, neurotransmitter reuptake, G protein-coupled receptors, G proteins, second messengers, the enzymes that trigger protein phosphorylation in response to cAMP, consequent metabolic processes such as glycogenolysis. Prominent examples include: The 1947 Nobel Prize in Physiology or Medicine to Carl Cori, Gerty Cori and Bernardo Houssay, for their discovery of how glycogen is broken down to glucose and resynthesized in the body, for use as a store and source of energy. Glycogenolysis is stimulated by numerous neurotransmitters including adrenaline; the 1970 Nobel Prize in Physiology or Medicine to Julius Axelrod, Bernard Katz and Ulf von Euler for their work on the release and reuptake of neurotransmitters. The 1971 Nobel Prize in Physiology or Medicine to Earl Sutherland for discovering the key role of adenylate cyclase, which produces the second messenger cyclic AMP; the 1988 Nobel Prize in Physiology or Medicine to George H. Hitchings, Sir James Black and Gertrude Elion "for their discoveries of important principles for drug treatment" targeting GPCRs.
The 1992 Nobel Prize in Physiology or Medicine to Edwin G. Krebs and Edmond H. Fischer for describing how reversible phosphorylation works as a switch to activate proteins, to regulate various cellular processes including glycogenolysis; the 1994 Nobel Prize in Physiology or Medicine to Alfred G. Gilman and Martin Rodbell for their discovery of "G-proteins and the role of these proteins in signal transduction in cells"; the 2000 Nobel Prize in Physiology or Medicine to Eric Kandel, Arvid Carlsson and Paul Greengard, for research on neurotransmitters such as dopamine, which act via GPCRs. The 2004 Nobel Prize in Physiology or Medicine to Richard Axel and Linda B. Buck for their work on G protein-coupled olfactory receptors; the 2012 Nobel Prize in Chemistry to Brian Kobilka and Robert Lefkowitz for their work on GPCR function. G proteins are important signal transducing molecules in cells. "Malfunction of GPCR signaling pathways are involved in many diseases, such as diabetes, allergies, cardiovascular defects, certain forms of cancer.
It is estimated that about 30% of the modern drugs' cellular targets are GPCRs." The human genome encodes 800 G protein-coupled receptors, which detect photons of light, growth factors and other endogenous ligands. 150 of the GPCRs found in the human genome have still-unknown functions. Whereas G proteins are activated by G protein-coupled receptors, they are inactivated by RGS proteins. Receptors stimulate GTP binding. RGS proteins stimulate GTP hydrolysis. All eukaryotes has evolved a large diversity of G proteins. For instance, humans encode 18 different Gα proteins, 5 Gβ proteins, 12 Gγ proteins. G protein can refer to two distinct families of proteins. Heterotrimeric G proteins, sometimes referred to as the "large" G proteins, are activated by G protein-coupled receptors and are made up of alpha and gamma subunits. "Small" G proteins belong to the Ras superfamily of small GTPases. These proteins are homologous to the alpha subunit found in heterotrimers, but are in fact monomeric, consisting of only a single unit.
However, like their larger relatives, they al
Leishmania is a genus of trypanosomes that are responsible for the disease leishmaniasis. They are spread by sandflies of the genus Phlebotomus in the Old World, of the genus Lutzomyia in the New World. At least 93 sandfly species are probable vectors worldwide, their primary hosts are vertebrates. The first written reference to the conspicuous symptoms of cutaneous leishmaniasis surfaced in the Paleotropics within oriental texts dating back to the 7th century BC. Due to its broad and persistent prevalence throughout antiquity as a mysterious disease of diverse symptomatic outcomes, leishmaniasis has been dubbed with various names ranging from "white leprosy" to "black fever"; some of these names suggest links to negative cultural beliefs or mythology, which still feed into the social stigmatization of leishmaniasis today. Members of an ancient genus of the Leishmania parasite, have been detected in fossilized sand flies dating back to the early Cretaceous period, the causative agent for the disease was only discovered in 1901 as a concurrent finding by William Boog Leishman and Charles Donovan.
They independently visualised microscopic single-celled parasites living within the cells of infected human organs. The parasitic genus would be classed as Trypanosomatid protozoans under the phylogenetic designation, Leishmania donovani. Several species have since been classified and grouped under two major subgenera i.e. Leishmania Viannia or Leishmania Leishmania. Leishmania affects 6 million people in 98 countries. About 0.9-1.6 million new cases occur each year, 21 species are known to cause disease in humans. Leishmania species are unicellular eukaryotes having a well-defined nucleus and other cell organelles including kinetoplasts and flagella. Depending on the stage of their lifecycle, they exist in two structural variants, as: The amastigote form is found in the mononuclear phagocytes and circulatory systems of humans, it is an nonmotile form, being devoid of external flagella. The short flagellum is embedded at the anterior end without projecting out, it is oval in shape, measures 3–6 µm in length and 1–3 µm in breadth.
The kinetoplast and basal body lie towards the anterior end. The promastigote form is found in the alimentary tract of sandflies, it is an motile form. It is larger and elongated, measuring 15-30 µm in length and 5 µm in width, it is spindle-shaped. A long flagellum is projected externally at the anterior end; the nucleus lies at the centre, in front of it are the kinetoplast and the basal body. The details of the evolution of this genus are debated, but Leishmania evolved from an ancestral trypanosome lineage; the oldest lineage is that of the Bodonidae, followed by Trypanosoma brucei, the latter being confined to the African continent. Trypanosoma cruzi groups with trypanosomes from bats, South American mammals, kangaroos suggest an origin in the Southern Hemisphere; these clades are only distantly related. The remaining clades in this tree are Blastocrithidia and Phytomonas; the four genera Leptomonas, Crithidia and Endotrypanum form the terminal branches, suggesting a recent origin. Several of these genera may need further division.
The origins of genus Leishmania itself are unclear. One theory proposes an African origin, with migration to the Americas. Another proposes migration from the Americas to the Old World via the Bering Strait land bridge around 15 million years ago. A third theory proposes a palearctic origin; such migrations would entail subsequent migration of vector and reservoir or successive adaptations along the way. A more recent migration is that of L. infantum from Mediterranean countries to Latin America, since European colonization of the New World, where the parasites picked up their current New World vectors in their respective ecologies. This is the cause of the epidemics now evident. One recent New World epidemic concerns foxhounds in the USA. Leishmania might have evolved in the Neotropics. A large data set; the reptile infecting species originated in mammalian clades. Sauroleishmania species were defined on the basis that they infected reptiles rather than mammals. Molecular studies have cast doubts on this basis for classification and they have been moved to subgenus status within Leishmania.
This subgenus evolved from a group that infected mammals. 53 species are recognised in this genus. The status of several of these is disputed, so the final number may differ. At least 20 species infect humans. To make things more complex, hybrids might be involved, as it has been reported in Brazil with an hybrid between Leishmania guyanensis and Leishmania shawi shawi. At least three subgenera exist: Leishmania and Viannia; the division into the two subgenera was made by Lainson and Shaw in 1987 on the basis of their location within the insect gut. The species in the Viannia subgenus develop in the hind gut: L. braziliensis has been proposed as the type species for this subgenus. This division has been confirmed by all subsequent studies. Endotrypanum is closely related and may be moved to subgenus status within Leishmania; the subgenus Endotypanum is unique in that the paras
Nucleic acids are the biopolymers, or small biomolecules, essential to all known forms of life. The term nucleic acid is the overall name for DNA and RNA, they are composed of nucleotides, which are the monomers made of three components: a 5-carbon sugar, a phosphate group and a nitrogenous base. If the sugar is a compound ribose, the polymer is RNA. Nucleic acids are the most important of all biomolecules, they are found in abundance in all living things, where they function to create and encode and store information in the nucleus of every living cell of every life-form organism on Earth. In turn, they function to transmit and express that information inside and outside the cell nucleus—to the interior operations of the cell and to the next generation of each living organism; the encoded information is contained and conveyed via the nucleic acid sequence, which provides the'ladder-step' ordering of nucleotides within the molecules of RNA and DNA. Strings of nucleotides are bonded to form helical backbones—typically, one for RNA, two for DNA—and assembled into chains of base-pairs selected from the five primary, or canonical, which are: adenine, guanine and uracil.
Using amino acids and the process known as protein synthesis, the specific sequencing in DNA of these nucleobase-pairs enables storing and transmitting coded instructions as genes. In RNA, base-pair sequencing provides for manufacturing new proteins that determine the frames and parts and most chemical processes of all life forms. Nuclein were discovered by Friedrich Miescher in 1869. In the early 1880s Albrecht Kossel further purifies the substance and discovers its acidic properties, he also identifies the nucleobases. In 1889 Richard Altmann creates the term nucleic acid In 1938 Astbury and Bell published the first X-ray diffraction pattern of DNA. In 1953 Watson and Crick determined the structure of DNA. Experimental studies of nucleic acids constitute a major part of modern biological and medical research, form a foundation for genome and forensic science, the biotechnology and pharmaceutical industries; the term nucleic acid is the overall name for DNA and RNA, members of a family of biopolymers, is synonymous with polynucleotide.
Nucleic acids were named for their initial discovery within the nucleus, for the presence of phosphate groups. Although first discovered within the nucleus of eukaryotic cells, nucleic acids are now known to be found in all life forms including within bacteria, mitochondria, chloroplasts and viroids.. All living cells contain both DNA and RNA, while viruses contain either DNA or RNA, but not both; the basic component of biological nucleic acids is the nucleotide, each of which contains a pentose sugar, a phosphate group, a nucleobase. Nucleic acids are generated within the laboratory, through the use of enzymes and by solid-phase chemical synthesis; the chemical methods enable the generation of altered nucleic acids that are not found in nature, for example peptide nucleic acids. Nucleic acids are very large molecules. Indeed, DNA molecules are the largest individual molecules known. Well-studied biological nucleic acid molecules range in size from 21 nucleotides to large chromosomes. In most cases occurring DNA molecules are double-stranded and RNA molecules are single-stranded.
There are numerous exceptions, however—some viruses have genomes made of double-stranded RNA and other viruses have single-stranded DNA genomes, and, in some circumstances, nucleic acid structures with three or four strands can form. Nucleic acids are linear polymers of nucleotides; each nucleotide consists of three components: a purine or pyrimidine nucleobase, a pentose sugar, a phosphate group. The substructure consisting of a nucleobase plus sugar is termed a nucleoside. Nucleic acid types differ in the structure of the sugar in their nucleotides–DNA contains 2'-deoxyribose while RNA contains ribose; the nucleobases found in the two nucleic acid types are different: adenine and guanine are found in both RNA and DNA, while thymine occurs in DNA and uracil occurs in RNA. The sugars and phosphates in nucleic acids are connected to each other in an alternating chain through phosphodiester linkages. In conventional nomenclature, the carbons to which the phosphate groups attach are the 3'-end and the 5'-end carbons of the sugar.
This gives nucleic acids directionality, the ends of nucleic acid molecules are referred to as 5'-end and 3'-end. The nucleobases are joined to the sugars via an N-glycosidic linkage involving a nucleobase ring nitrogen and the 1' carbon of the pentose sugar ring. Non-standard nucleosides are found in both RNA and DNA and arise from modification of the standard nucleosides within the DNA molecule or the primary RNA transcript. Transfer RNA molecules contain a large number of modified nucleosides. Double-stranded nucleic acids are made up of complementary sequences, in which extensive Watson-Crick base pairing results in a repeated and quite uniform double-helical three-dimensional structure. In contrast, single-stranded
Nitrogen is a chemical element with symbol N and atomic number 7. It was first discovered and isolated by Scottish physician Daniel Rutherford in 1772. Although Carl Wilhelm Scheele and Henry Cavendish had independently done so at about the same time, Rutherford is accorded the credit because his work was published first; the name nitrogène was suggested by French chemist Jean-Antoine-Claude Chaptal in 1790, when it was found that nitrogen was present in nitric acid and nitrates. Antoine Lavoisier suggested instead the name azote, from the Greek ἀζωτικός "no life", as it is an asphyxiant gas. Nitrogen is the lightest member of group 15 of the periodic table called the pnictogens; the name comes from the Greek πνίγειν "to choke", directly referencing nitrogen's asphyxiating properties. It is a common element in the universe, estimated at about seventh in total abundance in the Milky Way and the Solar System. At standard temperature and pressure, two atoms of the element bind to form dinitrogen, a colourless and odorless diatomic gas with the formula N2.
Dinitrogen forms about 78 % of Earth's atmosphere. Nitrogen occurs in all organisms in amino acids, in the nucleic acids and in the energy transfer molecule adenosine triphosphate; the human body contains about 3% nitrogen by mass, the fourth most abundant element in the body after oxygen and hydrogen. The nitrogen cycle describes movement of the element from the air, into the biosphere and organic compounds back into the atmosphere. Many industrially important compounds, such as ammonia, nitric acid, organic nitrates, cyanides, contain nitrogen; the strong triple bond in elemental nitrogen, the second strongest bond in any diatomic molecule after carbon monoxide, dominates nitrogen chemistry. This causes difficulty for both organisms and industry in converting N2 into useful compounds, but at the same time means that burning, exploding, or decomposing nitrogen compounds to form nitrogen gas releases large amounts of useful energy. Synthetically produced ammonia and nitrates are key industrial fertilisers, fertiliser nitrates are key pollutants in the eutrophication of water systems.
Apart from its use in fertilisers and energy-stores, nitrogen is a constituent of organic compounds as diverse as Kevlar used in high-strength fabric and cyanoacrylate used in superglue. Nitrogen is a constituent including antibiotics. Many drugs are mimics or prodrugs of natural nitrogen-containing signal molecules: for example, the organic nitrates nitroglycerin and nitroprusside control blood pressure by metabolizing into nitric oxide. Many notable nitrogen-containing drugs, such as the natural caffeine and morphine or the synthetic amphetamines, act on receptors of animal neurotransmitters. Nitrogen compounds have a long history, ammonium chloride having been known to Herodotus, they were well known by the Middle Ages. Alchemists knew nitric acid as aqua fortis, as well as other nitrogen compounds such as ammonium salts and nitrate salts; the mixture of nitric and hydrochloric acids was known as aqua regia, celebrated for its ability to dissolve gold, the king of metals. The discovery of nitrogen is attributed to the Scottish physician Daniel Rutherford in 1772, who called it noxious air.
Though he did not recognise it as an different chemical substance, he distinguished it from Joseph Black's "fixed air", or carbon dioxide. The fact that there was a component of air that does not support combustion was clear to Rutherford, although he was not aware that it was an element. Nitrogen was studied at about the same time by Carl Wilhelm Scheele, Henry Cavendish, Joseph Priestley, who referred to it as burnt air or phlogisticated air. Nitrogen gas was inert enough that Antoine Lavoisier referred to it as "mephitic air" or azote, from the Greek word άζωτικός, "no life". In an atmosphere of pure nitrogen, animals died and flames were extinguished. Though Lavoisier's name was not accepted in English, since it was pointed out that all gases are mephitic, it is used in many languages and still remains in English in the common names of many nitrogen compounds, such as hydrazine and compounds of the azide ion, it led to the name "pnictogens" for the group headed by nitrogen, from the Greek πνίγειν "to choke".
The English word nitrogen entered the language from the French nitrogène, coined in 1790 by French chemist Jean-Antoine Chaptal, from the French nitre and the French suffix -gène, "producing", from the Greek -γενής. Chaptal's meaning was that nitrogen is the essential part of nitric acid, which in turn was produced from nitre. In earlier times, niter had been confused with Egyptian "natron" – called νίτρον in Greek – which, despite the name, contained no nitrate; the earliest military and agricultural applications of nitrogen compounds used saltpeter, most notably in gunpowder, as fertiliser. In 1910, Lord Rayleigh discovered that an electrical discharge in nitrogen gas produced "active nitrogen", a monatomic allotrope of nitrogen; the "whirling cloud of brilliant yellow light