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
Amino acids are organic compounds containing amine and carboxyl functional groups, along with a side chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen and nitrogen, although other elements are found in the side chains of certain amino acids. About 500 occurring amino acids are known and can be classified in many ways, they can be classified according to the core structural functional groups' locations as alpha-, beta-, gamma- or delta- amino acids. In the form of proteins, amino acid residues form the second-largest component 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. In biochemistry, amino acids having both the amine and the carboxylic acid groups attached to the first carbon atom have particular importance, they are known as α-amino acids. They include the 22 proteinogenic amino acids, which combine into peptide chains to form the building-blocks of a vast array of proteins.
These are all L-stereoisomers, although a few D-amino acids occur in bacterial envelopes, as a neuromodulator, in some antibiotics. Twenty of the proteinogenic amino acids are encoded directly by triplet codons in the genetic code and are known as "standard" amino acids; the other two are selenocysteine, pyrrolysine. Pyrrolysine and selenocysteine are encoded via variant codons. N-formylmethionine is considered as a form of methionine rather than as a separate proteinogenic amino acid. Codon–tRNA combinations not found in nature can be used to "expand" the genetic code and form novel proteins known as alloproteins incorporating non-proteinogenic amino acids. Many important proteinogenic and non-proteinogenic amino acids have biological functions. For example, in the human brain and gamma-amino-butyric acid are the main excitatory and inhibitory neurotransmitters. Hydroxyproline, a major component of the connective tissue collagen, is synthesised from proline. Glycine is a biosynthetic precursor to porphyrins used in red blood cells.
Carnitine is used in lipid transport. Nine proteinogenic amino acids are called "essential" for humans because they cannot be produced from other compounds by the human body and so must be taken in as food. Others may be conditionally essential for medical conditions. Essential amino acids may differ between species; because of their biological significance, amino acids are important in nutrition and are used in nutritional supplements, fertilizers and food technology. Industrial uses include the production of drugs, biodegradable plastics, chiral catalysts; the first few amino acids were discovered in the early 19th century. In 1806, French chemists Louis-Nicolas Vauquelin and Pierre Jean Robiquet isolated a compound in asparagus, subsequently named asparagine, the first amino acid to be discovered. Cystine was discovered in 1810, although its monomer, 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 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. Usage of the term "amino acid" in the English language is from 1898, while the German term, Aminosäure, was used earlier. Proteins were found to yield amino acids after enzymatic 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". In the structure shown at the top of the page, R represents a side chain specific to each amino acid; the carbon atom next to the carboxyl group is called the α–carbon. Amino acids containing an amino group bonded directly to the alpha carbon are referred to as alpha amino acids; these include amino acids such as proline which contain secondary amines, which used to be referred to as "imino acids". The alpha amino acids are the most common form found in nature, but only when occurring in the L-isomer.
The alpha carbon is a chiral carbon atom, with the exception of glycine which has two indistinguishable hydrogen atoms on the alpha carbon. Therefore, all alpha amino acids but glycine can exist in either of two enantiomers, called L or D amino acids, which are mirror images of each other. While L-amino acids represent all of the amino acids found in proteins during translation in the ribosome, D-amin
Proteins are essential nutrients for the human body. They are one of the building blocks of body tissue and can serve as a fuel source; as a fuel, proteins provide as much energy density as carbohydrates: 4 kcal per gram. The most important aspect and defining characteristic of protein from a nutritional standpoint is its amino acid composition. Proteins are polymer chains made of amino acids linked together by peptide bonds. During human digestion, proteins are broken down in the stomach to smaller polypeptide chains via hydrochloric acid and protease actions; this is crucial for the absorption of the essential amino acids that cannot be biosynthesized by the body. There are nine essential amino acids which humans must obtain from their diet in order to prevent protein-energy malnutrition and resulting death, they are phenylalanine, threonine, methionine, isoleucine and histidine. There has been debate as to whether there are 9 essential amino acids; the consensus seems to lean towards 9. There are five amino acids.
These five are alanine, aspartic acid, glutamic acid and serine. There are six conditionally essential amino acids whose synthesis can be limited under special pathophysiological conditions, such as prematurity in the infant or individuals in severe catabolic distress; these six are arginine, glycine, glutamine and tyrosine. Dietary sources of protein include both animals and plants: meats, dairy products and eggs, as well as grains and nuts. Vegans can get enough essential amino acids by eating plant proteins. Protein is a nutrient needed by the human body for maintenance. Aside from water, proteins are the most abundant kind of molecules in the body. Protein can be found in all cells of the body and is the major structural component of all cells in the body muscle; this includes body organs and skin. Proteins are used in membranes, such as glycoproteins; when broken down into amino acids, they are used as precursors to nucleic acid, co-enzymes, immune response, cellular repair, other molecules essential for life.
Additionally, protein is needed to form blood cells. Protein can be found in a wide range of food; the best combination of protein sources depends on the region of the world, cost, amino acid types and nutrition balance, as well as acquired tastes. Some foods are high in certain amino acids, but their digestibility and the anti-nutritional factors present in these foods make them of limited value in human nutrition. Therefore, one must consider digestibility and secondary nutrition profile such as calories, cholesterol and essential mineral density of the protein source. On a worldwide basis, plant protein foods contribute over 60 percent of the per capita supply of protein, on average. In North America, animal-derived foods contribute about 70 percent of protein sources. Meat, products from milk, eggs and fish are sources of complete protein. Whole grains and cereals are another source of proteins. However, these tend to be limiting in the amino acid lysine or threonine, which are available in other vegetarian sources and meats.
Examples of food staples and cereal sources of protein, each with a concentration greater than 7.0%, are buckwheat, rye, maize, wheat, sorghum and quinoa. Vegetarian sources of proteins include legumes, nuts and fruits. Legumes, some of which are called pulses in certain parts of the world, have higher concentrations of amino acids and are more complete sources of protein than whole grains and cereals. Examples of vegetarian foods with protein concentrations greater than 7 percent include soybeans, kidney beans, white beans, mung beans, cowpeas, lima beans, pigeon peas, wing beans, Brazil nuts, pecans, cotton seeds, pumpkin seeds, hemp seeds, sesame seeds, sunflower seeds. Food staples that are poor sources of protein include roots and tubers such as yams and sweet potato. Plantains, another major staple, are a poor source of essential amino acids. Fruits, while rich in other essential nutrients, are another poor source of amino acids; the protein content in roots and fruits is between 0 and 2 percent.
Food staples with low protein content must be complemented with foods with complete, quality protein content for a healthy life in children for proper development. A good source of protein is a combination of various foods, because different foods are rich in different amino acids. A good source of dietary protein meets two requirements: The requirement for the nutritionally indispensable amino acids under all conditions and for conditionally indispensable amino acids under specific physiological and pathological conditions The requirement for nonspecific nitrogen for the synthesis of the nutritionally dispensable amino acids and other physiologically important nitrogen-containing compounds such as nucleic acids and porphyrins. Healthy people eating a balanced diet need protein supplements; the table below presents the most important food groups as protein sources, from a worldwide perspective. It lists their respective performance as source of the limiting amino acids, in milligrams of limiting amino acid per gram of total protein in the food source.
The table reiterates the need for a balanced mix of
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