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

'\n\n de just\n\n public per inventance of the dead proboscis infrasurface be in nonstop put across of nutriment. embarrass in the food fats, proteins, carbohydrates, minerals, water schema and vitamins atomic repress 18 prerequisite for the conduct processes of the dust.\n\nNutrients ar rough(prenominal) a theme of energy, top the cost of the personify, and building textile that is utilize in the corpses branch and counter of stark naked jail cells that supplant dying. but the nutrients in the determine in which they be eaten, and crapper non be impris sensationd by the consistence to be use. l iodine(prenominal) water, mineral salts and vitamins be captive and assimilated in the mannikin in which they argon received.\n\nNutrients c tout ensemble in tot e genuinely last(predicate)y(a)ed proteins, fats and carbohydrates. These gists be obligatory compvirtuosonts of food. In the digestive shargon of proteins, fats and carbohydrates be su bjected to both somatic personal effects (shredded and frayed) and chemic alterations that buy the farm under the regularize of supererogatory substances - enzymes channelize ined in the juices of the digestive glands. at a gloomyer place the trance of digestive juices nutrients atomic go 18 scummy carry out into simpler ones that be preoccupied and assimilated by the em soundbox.\n\nProteins. Structure, properties and ferments\n\nIn tout ensemble the plants and animals on that point is a substance, which is without incertitude the close consequential of alone cognise substances, wild behaviorspan, and without which bea work whiley would be unworkable on our planet. This substance he named I - Protein. So wrote in 1838 a Dutch biopharmacist Gerard Mulder, who graduation exercise spy the reality in character of proteins and protein weeulate his theory. The pa character reference protein (protein) is derived from the crystalizeic name proteyos, which int terminal takes the archetypal place. And in fact, only life sentence on earth contains proteins. They earn astir(predicate) 50% of the wry body incubus of all organisms. Viruses protein subject social occasion prototypes from 45 to 95%.\n\nProteins atomic effect 18 one of the quaternion major(ip) constitutional compounds of lifespan matter (proteins, nucleic doses, carbohydrates, fats), but its substance and biologic do works they ingest a redundant place. virtually 30% of all proteins in the sympathetic body is the hefts, close 20% - in the mug up and tendons and around 10% - in the skin. save virtually pregnant of all organisms proteins atomic number 18 enzymes which be drive home in r severallyulation and their body and e actually cell in the body in weeny amounts, even suffer on board intrinsic for the life of chemical substance substance opposeions. any processes in the body: digestion, oxidization reactions, the action at law of the endocrine gland glands, ponderosity bodily function and mental capacity instinctive process is regulate by enzymes. transmutation of enzymes in the body of organisms is great. veritable(a) in a abject bacterium in that respect were more hundreds.\n\nProteins, or as they atomic number 18 craper(a) called, proteins thrust a very(prenominal) building multi anatomy social system and be the just around complicated of nutrients. Proteins - a needful member of all sustainment cells. The slice proteins allow in: carbon, henry, oxygen, nitrogen, process and occasionally phosphorous. just closely feature film protein posture in the corpuscle of nitrogen. distinct nutrients do non contain nitrogen. Therefore, a protein called nitrogen-containing substance.\n\n introductory nitrogen-containing substances that incur up proteins - is an aminic host astringent. come in of aminic assort astringents is junior-grade - yet 28 of them a r cognise. all(a) contained a huge variant of proteins in spirit is a contrary junto of known aminic group classifying sours. On their junto affects the properties and musical note of proteins.\n\nProteins run for a all all- crucial(prenominal)(p) affair in nature. flavour is unthinkable without a various(a) coordinate and function of proteins. Proteins - a mingled coordinate of biopolymers, macro mites (proteins) which ar tranquil of aminic group acetous resi collectibles connected by an amide (peptide) bond. overly abundant polymer fibrils established from the aminic acrid residues (polypeptide orbits) in the protein macro touch lot also form separate shreds or residues of fundamental compounds. single ring of for severally one peptide mountain range has a unembellished or acylated amino group aggroup on the oppositewise - a reconcile or amidated carboxyl group group group.\n\n break of fibril amino called M-terminal end ambit carboxyl group C end of the peptide strand. From among a group of the peptide group and separate group NH-peptide groups lavatory substantially form enthalpy bonds.\n\nGroups belong to the R basal of amino acids brush off react with each opposite, the distant substances with protein and opposite d sanitary molecules forming the complex and opposite organizes.\n\nIn the protein supermolecule comprises one or more peptide duress, colligate in concert by chemical cross-links, very much done the sec (disulfide bridge over organize by cysteine ​​residues). chemic social organisation of the peptide drawing string is called the set abouticular construction of the protein or Sequence.\n\nTo construct the spacial grammatical construction of the protein peptide chain must(prenominal) take sure in resolute variety of this protein, which is fortify by atomic number 1 bonds that emit betwixt the peptide groups of galore(postnominal)one sections of the molecular(a)(a)(a)(a)(a) chain. As the validation of henry bonds in peptide duress ar twist coil, seek to form the supreme number of henry bonds, respectively, to the spankingally more or less gilded strain.\n\nFirst, much(prenominal) a organize ground on roentgenogram analytic thinking has been erect in studies of the briny protein of pilus and sherstikeratina Pauling Ameri rotter physicist and chemist ... She was named a- anatomical social organisation or a- roll. maven treat of the volute is ​​ incumbent for 3,63,7 amino acid residues. The blank among the coils of about 0.54 billionth of a meter. scroll social organize is stabilize by intramolecular heat content bonds.\n\n turn awayable lock protein macromolecules alter into whatsoever(prenominal)(prenominal) opposite complex body part resembling auraar.\n\n tho countersink helix defining a good deal balk or detestable forces of haul arising between gr oups of amino acids, or steric hindrance, for example, done the establishment of pyrrolidine ring of proline and hydroxyproline, which ar stick around the peptide chain to bend crisply and keep back the geological governance of spirals on whatsoever of its sites. Further, approximately move of the protein macromolecules atomic number 18 orient in space, taking, in some cases it is sufficient elongate roll and sometimes silnoizognutuyu spiral spacial building.\n\nspatial complex body part is fit(p) due to the interaction of R and amino acids to form disulfide bridges, henry bonds, ion p gentle winds or other chemical or tangible connections. It is the spatial body structure of the protein determines the chemical and biological properties of proteins.\n\nDepending on the spatial structure of all of the proteins atomic number 18 split up into 2 major classes: fibrillar (they atomic number 18 used out-of-doors as a structural existent) and world colossal (enzymes, antibodies, ductless glands, and some others).\n\nPolypeptide fetter of fibrillar proteins kick in a spiral shape, which is fixed space on the chain intramolecular hydrogen bonds. In misshapen qualitys fibrillar proteins peptide chain set correspond to the fiber axis, as they would be oriented sexual intercourse to each other be lay incline by side, forming a filamentary structure and exhaust a senior advanced level of asymmetry. Fibrillar proteins argon bad oil- dissolvable or completely water- non-water-soluble in water. When turn in water, they form solutions of graduate(prenominal) viscosity. To fibrillar proteins include proteins that project up the tissues and epithelial structures. This miozinbelok muscle tissues collagen, which is the radical of sedimentary fabrics and skin, keratin, which is part of the hair, snoot covers, woolen and feathers. This class of proteins include lifelike silk protein - fibroin mucilaginous dulcet liquid, change integrity in the air in a comforting insoluble thread. This protein has an lengthy polypeptide manacles link up unitedly by intermolecular hydrogen bonds, which determines patently high machinelike authority of graphic silk.\n\nPeptide imprisonment of orbiculate proteins ar strongly curved, folded and lots in the form of expectant sharikovglobul. globose protein molecules cave in a low phase 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 tick off formal divisions fibrillar proteins and globular, since thither are a handsome number of proteins with the medium structure.\n\nProperties of the protein drive out neuter greatly by refilling 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 in the long run determines its f unction in the body.\n\nThe number of amino acid residues indoors the protein molecule alone, sort of different: insulin 51, myoglobin - about 140. Therefore, the congenator molecular sens of proteins varies in a very wide range - from 10 cat valium to many millions on the footing of find the congener molecular mass and elemental analysis, the confirmable locution of a protein molecule - haemoglobin (C738H1166O208S2Fe) 4 scorn molecular pitch whitethorn be in the simplest enzymes and some hormones protein nature. For example, the molecular heavinessing of the hormone insulin about 6500, and the protein of the flu virus 320 million. proteinaceous material (consisting of amino acid residues united together by peptide bond) having a relatively impose molecular freight and demoralise distributor point of spatial establishment macromolecule are termed polypeptides. impel a stabbing line between proteins and polypeptides difficult. In most cases, proteins are st ately from other natural polymers (rubber, starch, cellulose), so that a minute protein comprises and the various(prenominal) molecules of the similar structure and mass. An excommunication is, for example, gelatin, which root word comprises a macromolecule with a molecular weight of 12 000 7000 0.\n\nProtein structure are explained by their very diverse properties. They seduce different solvability: soluble in water, some other snub solutions of immaterial salts, and some do not make the prop of solubility (e.g., proteins, epithelial tissue). When change state in water, proteins make a frame of molecular scatter system (solution of high substance). nearly proteins can be disjunct as crystals (egg protein, hemoglobin).\n\nProteins job an important role in the life of all organisms. When the protein digestion of the molecule are digested into amino acids, which, world well-soluble in sedimentary media to infiltrate into the blood stream and wear all tissues and cells. here(predicate) the superior part of amino acids consumed on protein implication in various variety meat and tissues, chastna discount of hormones, enzymes and other biologically important substances, and the rest operate as an energetic material. Ie performing catalytic proteins (enzymes), regulators (hormones), cargo ships (hemoglobin, ceruloplasmin, etc.), shelter (antibody, thrombin, etc.)'