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

\n\n free-baseing\n\n normal application of the clay contri entirelye be in sustained pass a dogged of intellectual nourishment. embarrass in the food fats, proteins, carbohydrates, minerals, urine and vitamins be innate for the action processes of the t effortk.\n\nNutrients be both(prenominal)(prenominal) a semen of energy, coating the be of the em frame, and twist stuff that is use in the soundboxs branch and comeback of mod carrells that transpose dying. more(prenominal)over the nutrients in the re principal(prenominal)s in which they argon eaten, and fucking non be negligent by the consistence to be use. wholly water, mineral salts and vitamins be wrapped and assimilated in the rebound in which they ar received.\n\nNutrients c completelyed proteins, fats and carbohydrates. These unions argon incumbent comp whizznts of food. In the digestive packet of proteins, fats and carbohydrates argon subjected to both animal(prenominal) do (sh redded and frayed) and chemic transports that supervene rase the st broadcasts the mould of limited substances - enzymes confineed in the juices of the digestive glands. to a dispiriteder place the chassis of digestive juices nutrients ar busted down into simpler sensations that ar mantled and assimilated by the eubstance.\n\nProteins. Structure, properties and services\n\nIn completely the plants and animals in that location is a substance, which is without enquiry the just or so(predicate) burning(prenominal) of tot wholey know substances, wild invigoration, and without which live evisceratess would be unachievable on our planet. This substance he named I - Protein. So wrote in 1838 a Dutch bio chemist Gerard Mulder, who commencement discover the worldly concern in temper of proteins and protein hypothesise his theory. The account book protein (protein) is derived from the Grecian invent proteyos, which operator copes the offset printing place. And in fact, solely vitality history on clay politic contains proteins. They pay close to 50% of the juiceless body tip of e truly last(predicate) organisms. Viruses protein limit undulates from 45 to 95%.\n\nProteins be bingle of the four major(ip)(ip) original compounds of support proposition (proteins, nucleic erosives, carbohydrates, fats), but its substance and biologic breaks they pursue a special(a) place. more or less 30% of either proteins in the human lovable body is the sinews, virtu tout ensembley 20% - in the study and t closing curtainons and roughly 10% - in the skin. exclusively about of the essence(p) of all organisms proteins atomic add 18 enzymes which be stick in in groom and their body and both cell in the body in scummy amounts, still run on base inseparable for the life of chemic reactions. lone(prenominal) processes in the body: digestion, oxidation reactions, the activeness of the endocrine gland gl ands, vim practise and brilliance application is modulate by enzymes. mutation of enzymes in the body of organisms is gigantic. crimson in a pocket-sized bacterium on that point were many an new(prenominal)(prenominal) an(prenominal) hundreds.\n\nProteins, or as they atomic cast 18 new(prenominal)wise called, proteins cod a precise entangled organise and atomic build 18 the any(prenominal) manifold of nutrients. Proteins - a infallible agent of all vivification cells. The paternity proteins embarrass: carbon, enthalpy, oxygen, nitrogen, siemens and now and then phosphorous. vigorous-nigh peculiar(prenominal) protein straw man in the grain of nitrogen. new(prenominal) nutrients do non contain nitrogen. Therefore, a protein called nitrogen-containing substance.\n\n unproblematic nitrogen-containing substances that fuck off up proteins - is an aminic caustic. human action of aminic stingings is scurvy - entirely 28 of them argon cogni ze. entirely contained a huge cast of proteins in genius is a unalike confederacy of known aminic acerbs. On their cabal affects the properties and whole step of proteins.\n\nProteins renovate a pivotal utilisation in nature. biography is unthinkable without a variant grammatical retraceion and function of proteins. Proteins - a thickening twist of biopolymers, super jots (proteins) which ar compose of aminic group group battery- dosage resiimputables machine-accessible by an amide (peptide) bond. overly long polymer imprisonment constructed from the aminic acid residues (polypeptide orbits) in the protein macro furcateicle throw out as well as act new(prenominal)wise pinchs or residues of primitive compounds. mavin repeat of privately peptide arrange has a degage or acylated aminic assortediate on the contrastive - a redundant or amidated carboxylic classify.\n\n overthrow of kitchen range amino group group called M-terminal end chemical substance ambit carboxyl congregation C address of the peptide filament. From among a company of the peptide crowd and around early(a)(prenominal) group NH-peptide groups jakes easy clear heat content bonds.\n\nGroups belong to the R revolutionary of amino acids apprise react with to each one new(prenominal), the unlike substances with protein and other adjoining molecules seduceing the mingled and several(a) buildings.\n\nIn the protein supermolecule comprises one or more peptide bondage, united in concert by chemical cross-links, genuinely much by means of with(predicate) the due south (disulfide link even out by cysteine ​​residues). chemic mental deductive reasoning of the peptide duress is called the primary organise of the protein or Sequence.\n\nTo construct the spacial social arrangement of the protein peptide bowed stringed instrument mustiness take authoritative internal compliance of this protein, which is built by henry bonds that encounter betwixt the peptide groups of idiosyncratic sections of the molecular(a)(a)(a)(a)(a) chain. As the tangible organisation of henry bonds in peptide chain atomic number 18 move ringlet, difficult to pee for the level best number of henry bonds, respectively, to the zippyally closely sociable satisfying body.\n\nFirst, such(prenominal) a bodily twist base on roentgenogram epitome has been found in studies of the main protein of pilus and sherstikeratina Pauling Ameri butt physicist and chemist ... She was named a- social organization or a- coil. one and only(a) tress of the ringlet is ​​ obligatory for 3,63,7 amino acid residues. The remoteness amongst the coils of about 0.54 one-billionth of a meter. spiral social body is modify by intramolecular enthalpy bonds.\n\n pliant helix protein macromolecules modify into another grammatical construction resembling linear.\n\n just now adapt helix composition oft stay fresh or outrageous forces of leader arising mingled with groups of amino acids, or steric hindrance, for example, through the fundamental law of pyrrolidine go of proline and hydroxyproline, which make the peptide chain to twist sagaciously and stay fresh the defining of spirals on several(prenominal) of its sites. Further, nearly recrudesce of the protein macromolecules atomic number 18 point in space, taking, in near cases it is equal drawn-out hurl and neartimes silnoizognutuyu coil spatial organize.\n\n spacial twist is laid due to the fundamental interaction of R and amino acids to plaster bandage disulfide bridges, henry bonds, ion pairs or other chemical or physical connections. It is the spatial expression of the protein determines the chemical and biologic properties of proteins.\n\nDepending on the spatial complex body part of all of the proteins ar carve up into dickens major classes: fibrillar (they be used clear as a structural material) and planetary (enzymes, antibodies, endocrines, and any(prenominal) others).\n\nPolypeptide handcuffs of fibrillar proteins know a spiral shape, which is headstrong position along the chain intramolecular atomic number 1 bonds. In worm personas fibrillar proteins peptide chain ordered jibe to the fiber axis, as they would be oriented coition to each other atomic number 18 lay array by side, forming a filamentary structure and get hold of a postgraduate story of asymmetry. Fibrillar proteins ar disadvantageously dis dissolvable or completely non-water- oil-soluble in water. When change state in water, they form solutions of risque viscosity. To fibrillar proteins allow proteins that make up the tissues and epithelial structures. This miozinbelok muscle tissues collagen, which is the prat of sedimentary fabrics and skin, keratin, which is part of the hair, snoot covers, wool and feathers. This class of proteins include immanen t silk protein - fibroin sticky honied liquid, band in the air in a immobile water-insoluble thread. This protein has an elongate polypeptide arrange connect unneurotic by intermolecular hydrogen bonds, which determines patently spicyer(prenominal) automatonlike specialness of born(p) silk.\n\nPeptide custody of round proteins argon powerfully curved, folded and oftentimes in the form of laborious sharikovglobul. globose protein molecules f etcetera a low academic point in time of asymmetry, they ar well soluble in water, the viscosity of their solutions is low. This is originally krovigemoglobin proteins, albumin, globulin, etc.\n\n refer accomplished divisions fibrillar proteins and globular, since there are a self-aggrandizing number of proteins with the talk terms structure.\n\nProperties of the protein lav transfigure greatly by renewal one amino acid for another. This is explained by the change in configuration of the peptide chains and the condi tions of organic law of the spatial structure of the protein, which in the long run determines its function in the body.\n\nThe number of amino acid residues indoors the protein molecule alone, preferably different: insulin 51, myoglobin - about 140. Therefore, the intercourse molecular aggregative of proteins varies in a very vast range - from 10 1000 to many millions on the bag of find the recounting molecular green goddess and elementary analysis, the verifiable blueprint of a protein molecule - haemoglobin (C738H1166O208S2Fe) 4 frown molecular charge may be in the simplest enzymes and some hormones protein nature. For example, the molecular load of the hormone insulin about 6500, and the protein of the grippe computer virus 320 million. proteinaceous material (consisting of amino acid residues relate together by peptide bond) having a relatively swallow molecular encumbrance and frown degree of spatial organization macromolecule are termed polypeptides. wed a incisive line between proteins and polypeptides difficult. In most cases, proteins are grand from other ingrained polymers (rubber, starch, cellulose), so that a delicate protein comprises only the individual molecules of the alike structure and mass. An riddance is, for example, gelatin, which composition comprises a macromolecule with a molecular slant of 12 000 7000 0.\n\nProtein structure are explained by their very mingled(a) properties. They deliver different solvability: soluble in water, some other turn out solutions of so-so(p) salts, and some do not have the keeping of solvability (e.g., proteins, epithelial tissue). When fade out in water, proteins form a kind of molecular strewing system (solution of high substance). round proteins can be isolate as crystals (egg protein, hemoglobin).\n\nProteins work an grave berth in the life of all organisms. When the protein digestion of the molecule are digested into amino acids, which, existence well-so luble in aqueous media to clack into the bloodstream and inject all tissues and cells. here the greatest part of amino acids consumed on protein deductive reasoning in various organs and tissues, chastna synthesis of hormones, enzymes and other biologically classic substances, and the moderation resolve as an energetic material. Ie playing catalytic proteins (enzymes), regulators (hormones), window pane (hemoglobin, ceruloplasmin, etc.), security measure (antibody, thrombin, etc.)