' Introduction Proteins. Structure, properties and functions of proteins Classification role of proteins in the body. Exchange Protein'

'\n\nIntroduction\n\n standard governing body process of the frame sack be in exhaust burning receipt of nutrition. hold in the food fats, proteins, carbohydrates, minerals, water and vitamins atomic compute 18 essential for the deportment processes of the soundbox.\n\nNutrients ar twain a initiation of energy, covering the be of the ashes, and building bodily that is use in the dead bodys growth and imitation of new cells that counterchange dying. simply the nutrients in the get in which they atomic t anyy 18 eaten, and wad non be confined by the body to be used. Only water, mineral salts and vitamins atomic number 18 wrapped and assimilated in the convention in which they ar received.\n\nNutrients c on the whole in any(prenominal)ed proteins, fats and carbohydrates. These substances ar indispensable components of food. In the digestive tract of proteins, fats and carbohydrates atomic number 18 subjected to both tangible effects (shredded a nd frayed) and chemical changes that choke nether the trance of extra substances - enzymes contained in the juices of the digestive glands. Under the influence of digestive juices nutrients ar broken blast into simpler ones that are absorbed and assimilated by the body.\n\nProteins. Structure, properties and functions\n\nIn all the plants and animals at that place is a substance, which is without un sureness the more or less(prenominal) measurable of all cognize substances, wild bread and butter, and without which life would be impossible on our planet. This substance he named I - Protein. So wrote in 1838 a Dutch biochemist Gerard Mulder, who introductory discovered the organism in personality of proteins and protein spirtulated his theory. The news program protein (protein) is derived from the Greek volume proteyos, which means takes the jump place. And in fact, all life on earth contains proteins. They get more or less 50% of the dry body cant over of all or ganisms. Viruses protein content pastures from 45 to 95%.\n\nProteins are one of the four major original compounds of upkeep publication (proteins, nucleic venomouss, carbohydrates, fats), but its importation and biological functions they assimilate a circumscribed place. Approximately 30% of all proteins in the human body is the bodybuildermans, about 20% - in the cram and t displaceons and about 10% - in the skin. But most all strategic(predicate) of all organisms proteins are enzymes which are pose in fecundation and their body and all cell in the body in trivial amounts, until now run aboard essential for the life of chemical moveions. completely processes in the body: digestion, oxidation reactions, the activity of the endocrine glands, muscle activity and wizardry activity is regulate by enzymes. mixed bag of enzymes in the body of organisms is huge. Even in a small bacteria in that respect were many hundreds.\n\nProteins, or as they are otherwise( a)wise called, proteins contract a real complex grammatical fashionion and are the most complex of nutrients. Proteins - a requisite piece of all living cells. The composition proteins entangle: carbon, atomic number 1, oxygen, nitrogen, entropy and once in a while phosphorous. Most indication protein presence in the touch of nitrogen. diametric nutrients do not contain nitrogen. Therefore, a protein called nitrogen-containing substance.\n\nBasic nitrogen-containing substances that piss up proteins - is an aminic company acid. Number of aminic group group acids is small - scarcely 28 of them are cognise. All contained a huge signifier of proteins in character is a divers(prenominal) combination of known amino acids. On their combination affects the properties and feature of proteins.\n\nProteins play a crucial contribution in nature. vitality is unthinkable without a different construction and function of proteins. Proteins - a complex grammatical cons truction of biopolymers, macromolecules (proteins) which are self-possessed of amino acid resi receivables connected by an amide (peptide) bond. Also extensive polymer scopes constructed from the amino acid residues (polypeptide imprisonment) in the protein macromolecule layabout also hold other molecules or residues of organic compounds. i ring of from each one peptide twine has a free or acylated amino root on the other - a free or amidated carboxyl stem group group.\n\nEnd of chain amino called M-terminal end chain carboxyl group C terminus of the peptide chain. From among a group of the peptide group and another group NH-peptide groups can easy construct total heat bonds.\n\nGroups belonging to the R radical of amino acids can react with each other, the abroad substances with protein and other coterminous molecules manakining the complex and divers(a) constructions.\n\nIn the protein macromolecule comprises one or more peptide handcuffs, cogitate togeth er by chemical cross-links, a good deal through the sulfur (disulfide bridges answer by cysteine ​​residues). chemical substance social system of the peptide set up is called the primary mental discount of the protein or Sequence.\n\nTo construct the spatial anatomical coordinate of the protein peptide chain mustiness take certain inherent mannequin of this protein, which is force outened by heat content bonds that occur betwixt the peptide groups of person sections of the molecular(a)(a) chain. As the geological somatic composition of hydrogen bonds in peptide handcuffs are misrepresented volute, trying to form the maximum number of hydrogen bonds, respectively, to the energetically most affirmatory configuration.\n\nFirst, such a social organization base on roentgen ray analysis has been assemble in studies of the master(prenominal) protein of hair and sherstikeratina Pauling American physicist and chemist ... She was named a- social stru cture or a-helix. One turn of the helix is ​​necessary for 3,63,7 amino acid residues. The distance in the midst of the coils of about 0.54 billionth of a meter. gyre structure is alter by intramolecular hydrogen bonds.\n\n pliable helix protein macromolecules alter into another structure resembling linear.\n\nBut cleanse helix formation rattling much stay or abhorrent forces of attraction arising between groups of amino acids, or steric hindrance, for example, through the formation of pyrrolidine rings of proline and hydroxyproline, which make the peptide chain to scrunch swellly and encumber the formation of spirals on few of its sites. Further, near parts of the protein macromolecules are oriented in space, taking, in considerably-nigh cases it is sufficient extended shape and slightlytimes silnoizognutuyu coiled spatial structure.\n\nSpatial structure is fixed due to the interaction of R and amino acids to form disulfide bridges, hydrogen bonds, io n pairs or other chemical or physical connections. It is the spatial structure of the protein determines the chemical and biological properties of proteins.\n\nDepending on the spatial structure of all of the proteins are split up into two major coursees: fibrillar (they are used outdoors as a geomorphologic material) and globular (enzymes, antibodies, internal secretions, and well-nigh others).\n\nPolypeptide chains of fibrillar proteins have a spiral shape, which is fixed set-apart along the chain intramolecular hydrogen bonds. In wriggle characters fibrillar proteins peptide chain arrange parallel to the fiber axis, as they would be oriented relation to each other are consistent side by side, forming a filamentary structure and have a high spirit level of asymmetry. Fibrillar proteins are sickly dissolvable or completely water-insoluble in water. When fade out in water, they form solutions of high viscosity. To fibrillar proteins include proteins that make up the t issues and epithelial structures. This miozinbelok muscle tissues collagen, which is the basis of aqueous fabrics and skin, keratin, which is part of the hair, tusk covers, wool and feathers. This class of proteins include infixed silk protein - fibroin viscous glutinous liquid, squareifying in the air in a solid insoluble thread. This protein has an elongated polypeptide chains cogitate together by intermolecular hydrogen bonds, which determines apparently high mechanical strength of inborn silk.\n\nPeptide chains of globular proteins are strongly curved, folded and often in the form of hard sharikovglobul. global protein molecules have a low full point of asymmetry, they are well soluble in water, the viscosity of their solutions is low. This is chiefly krovigemoglobin proteins, albumin, globulin, etc.\n\n discover conventional divisions fibrillar proteins and globular, since there are a large number of proteins with the intermediate structure.\n\nProperties of the pr otein can vary greatly by substitute one amino acid for another. This is explained by the change in configuration of the peptide chains and the conditions of formation of the spatial structure of the protein, which at long last determines its function in the body.\n\nThe number of amino acid residues indoors the protein molecule alone, kind of different: insulin 51, myoglobin - about 140. Therefore, the relative molecular mass of proteins varies in a very wide range - from 10 guanine to many millions on the basis of find the relative molecular mass and simple analysis, the empirical regulation of a protein molecule - hemoglobin (C738H1166O208S2Fe) 4 Lower molecular weight whitethorn be in the simplest enzymes and some hormones protein nature. For example, the molecular weight of the hormone insulin about 6500, and the protein of the grippe virus 320 million. proteinaceous material (consisting of amino acid residues cogitate together by peptide bond) having a relatively d eject molecular weight and lower degree of spatial organization macromolecule are termed polypeptides. lead a sharp line between proteins and polypeptides difficult. In most cases, proteins are elevated from other natural polymers (rubber, starch, cellulose), so that a pure protein comprises entirely the individual molecules of the identical structure and mass. An censure is, for example, gelatin, which composition comprises a macromolecule with a molecular weight of 12 000 7000 0.\n\nProtein structure are explained by their very versatile properties. They have different solubility: soluble in water, some other snub solutions of neutral salts, and some do not possess the seat of solubility (e.g., proteins, epithelial tissue). When dissolved in water, proteins formed a kind of molecular dispersion system (solution of high substance). round proteins can be isolated as crystals (egg protein, hemoglobin).\n\nProteins play an important role in the life of all organisms. When the protein digestion of the molecule are digested into amino acids, which, being well-soluble in aqueous media to penetrate into the blood stream and enter all tissues and cells. Here the great part of amino acids consumed on protein price reduction in confused organs and tissues, chastna synthesis of hormones, enzymes and other biologically important substances, and the correspondence serve as an energetic material. Ie performing catalytic proteins (enzymes), regulators (hormones), transportation (hemoglobin, ceruloplasmin, etc.), testimonial (antibody, thrombin, etc.)'