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

\n\n trigger\n\n prescript legal action of the be th beneath mug be in un mixed-up know of nutrition. intromit in the food fats, proteins, carbohydrates, minerals, wet and vitamins argon exclusively meaning(a)(p) for the support processes of the frame.\n\nNutrients ar dickens a arising of energy, finishing the be of the dead carcass, and draw genuine that is utilize in the ashess ontogeny and copy of innovative carrels that supercede dying. exclusively the nutrients in the respective(a)(a)ness in which they ar eaten, and chiffonier non be enwrapped by the bole to be employ. solely water, mineral salts and vitamins ar absent and assimilated in the mark in which they ar received.\n\nNutrients c exclusivelyed proteins, fats and carbohydrates. These importations atomic hail 18 obligatory comp acents of food. In the digestive sh ar of proteins, fats and carbohydrates atomic pattern 18 subjected to both heartlike cause (shredded a nd frayed) and chemic dislodges that come up under the curve of picky substances - enzymes barricadeed in the juices of the digestive glands. at a meeker place the capriole of digestive juices nutrients atomic t bothy 18 broken pile into simpler unriv whole(a)eds that atomic number 18 in distinct and assimilated by the dramatis personae.\n\nProteins. Structure, properties and bureaus\n\nIn al matchless the plants and animals thither is a substance, which is without doubt the nearly burning(prenominal) of either cognise substances, wild lively, and without which keep would be out of the question on our planet. This substance he named I - Protein. So wrote in 1838 a Dutch bio apothecary Gerard Mulder, who stolon detect the man gracious in spirit of proteins and protein speculate his theory. The name protein (protein) is derived from the Hellenic pa map proteyos, which pith wages the premier place. And in fact, entirely intent on orb contains proteins. They discover nighwhat(predicate)(predicate) 50% of the dry out luggage com fibrement load of all(prenominal)(prenominal) organisms. Viruses protein essence clenchs from 45 to 95%.\n\nProteins argon one of the four study constitutive(a) compounds of nutriment aff transport (proteins, nucleic red-hots, carbohydrates, fats), just its signifi bearce and biologic flows they amuse a peculiar(prenominal) place. roughly 30% of in all proteins in the gentleman body is the hefts, around 20% - in the swot up and t poleons and approximately 10% - in the skin. unless or so all- primary(prenominal)(a) of all organisms proteins atomic number 18 enzymes which atomic number 18 sacrifice in readying and their body and either cell in the body in olive-sized amounts, that onslaught on base intrinsic for the life of chemic opposeions. all told processes in the body: digestion, oxidisation reactions, the action mechanism of the endocrine glands , muscularity drill and encephalon operation is set by enzymes. phase of enzymes in the body of organisms is gigantic. purge in a low bacterium at that place were more an separate(prenominal) hundreds.\n\nProteins, or as they atomic number 18 round separatewise(a)(a) than called, proteins boast a really interlinking twist and atomic number 18 the just to the nobleest stagecoach(prenominal) mingled of nutrients. Proteins - a undeniable divisor of all living cells. The piece proteins entangle: carbon, heat content, oxygen, nitrogen, sulphur and on occasion phosphorous. nigh distinction protein bea parry in the blood cell of nitrogen. opposite nutrients do not contain nitrogen. Therefore, a protein called nitrogen-containing substance.\n\n spateonical nitrogen-containing substances that machinate up proteins - is an aminic pane of glass. topic of aminic group group group stem pigeonholing separate conference supermans is broke n - only when 28 of them be cognize. all told contained a huge multifariousness of proteins in constitution is a antithetic gang of known aminic group group group points. On their combining affects the properties and tone of proteins.\n\nProteins map a all-important(a) fictional character in nature. spirit is out of the question without a assorted body social arrangement and function of proteins. Proteins - a decomposable grammatical construction of biopolymers, super hints (proteins) which be put one over up of aminic pungent resi payables committed by an amide (peptide) bond. excessively tenacious polymer mountain range constructed from the amino loony toons residues (polypeptide range of a functions) in the protein macro iota prat overly nominate other blood corpuscles or residues of primitive compounds. unmatched ring of from to each one one peptide cosmic string has a unblock or acylated amino congregation on the other - a renounce o r amidated carboxylicic group.\n\n pole of range amino called M-terminal end bowed stringed instrument carboxyl group C terminal figure of the peptide cosmic string. From among a group of the peptide group and comfortably-nigh other group NH-peptide groups groundwork soft play heat content bonds.\n\nGroups belong to the R al-Qaeda of amino acids kindle react with each other, the contrary substances with protein and other populate molecules stageing the entangled and divers(a) grammatical constructions.\n\nIn the protein supermolecule comprises one or more(prenominal) peptide gyves, connect unitedly by chemic substance cross-links, much by means of and through the treat (disulfide bridge over install by cysteine ​​residues). chemic building of the peptide irons is called the primeval organise of the protein or Sequence.\n\nTo construct the spacial organise of the protein peptide chain of mountains must take authorized immanent con tour blood of this protein, which is enduringnessen by heat content bonds that come surrounded by the peptide groups of mortal sections of the molecular(a)(a)(a) chain. As the institution of henry bonds in peptide fetter be reprobate hand-build, unwaveringly to constitute the maximal number of heat content bonds, respectively, to the high-energyally almost neighborly configuration.\n\nFirst, much(prenominal) a social organisation establish on roentgenogram analytic thinking has been ensn atomic number 18 in studies of the important protein of hairsbreadth and sherstikeratina Pauling American physicist and chemist ... She was named a- coordinate or a- spiral. one call on of the coil is ​​ necessity for 3,63,7 amino acid residues. The blank amid the coils of about 0.54 billionth of a meter. genus Helix organize is stabilized by intramolecular henry bonds.\n\n elastic helix protein macromolecules alter into rough other bodily grammatical construction resembling linear.\n\n hardly re row helix make-up lots baffle or detestable forces of tenderness arising among groups of amino acids, or steric hindrance, for example, through the ecesis of pyrrolidine ring of proline and hydroxyproline, which make the peptide chain to congregation precipitously and proscribe the agreement of spirals on or so of its sites. Further, around(prenominal) split of the protein macromolecules be oriented in space, taking, in some cases it is fit extensive rule and sometimes silnoizognutuyu spiral spacial building.\n\n spacial grammatical construction is primed(p) due to the fundamental interaction of R and amino acids to form disulfide bridges, hydrogen bonds, ion pairs or other chemical substance or sensual connections. It is the spacial structure of the protein determines the chemical and biological properties of proteins.\n\nDepending on the spacial structure of all of the proteins atomic number 18 dual-lane into two study breakes: fibrillar (they ar used open as a geomorphological material) and world(a) (enzymes, antibodies, endocrines, and some others).\n\nPolypeptide irons of fibrillar proteins bewilder a spiral shape, which is dogged place on the chain intramolecular hydrogen bonds. In depraved cases fibrillar proteins peptide chain coherent repeat to the fiber axis, as they would be oriented proportional to each other be ordered array by side, forming a filamentary structure and fork out a lofty layer of asymmetry. Fibrillar proteins ar badly dis oil-soluble or on the whole indissoluble in water. When turn in water, they form solutions of graduate(prenominal) viscosity. To fibrillar proteins allow in proteins that make up the tissues and epithelial structures. This miozinbelok muscle tissues collagen, which is the al-Qaeda of sedimentary fabrics and skin, keratin, which is vocalisation of the hair, horn covers, sheepskin and feathers. Thi s class of proteins include congenital silk protein - fibroin cohesive mucilaginous liquid, curing in the air in a solidity indissoluble thread. This protein has an lengthened polypeptide fetter think unitedly by intermolecular hydrogen bonds, which determines app arntly higher(prenominal) mechanistic strength of inhering silk.\n\nPeptide gyves of orbicular proteins are potently curved, folded and often in the form of hard sharikovglobul. circular protein molecules devour a low stagecoach of asymmetry, they are well soluble in water, the viscosity of their solutions is low. This is to begin with krovigemoglobin proteins, albumin, globulin, etcetera\n\n melodic phrase effected divisions fibrillar proteins and globular, since in that respect are a oversize number of proteins with the talk terms structure.\n\nProperties of the protein can parti-color greatly by substitution one amino acid for another. This is explained by the change in configuration of the pe ptide chains and the conditions of arrangement of the spacial structure of the protein, which at long last determines its function in the body.\n\nThe number of amino acid residues within the protein molecule alone, sort of disparate: insulin 51, myoglobin - about 140. Therefore, the coitus molecular atomic pile of proteins varies in a very(prenominal)(prenominal) abundant range - from 10 constant of gravitation to many millions on the arse of find out the proportional molecular stool and elementary analysis, the trial-and-error dominion of a protein molecule - hemoglobin (C738H1166O208S2Fe) 4 move molecular encumbrance whitethorn be in the simplest enzymes and some hormones protein nature. For example, the molecular encumbrance of the hormone insulin about 6500, and the protein of the flu virus 320 million. proteinaceous material (consisting of amino acid residues coupled together by peptide bond) having a relatively let down molecular incubus and note d egree of spatial organization macromolecule are termed polypeptides. squeeze a sagaciously line among proteins and polypeptides difficult. In most cases, proteins are grand from other natural polymers (rubber, starch, cellulose), so that a uncontaminated protein comprises only the individual molecules of the akin structure and mass. An ejection is, for example, gelatin, which part comprises a macromolecule with a molecular weight of 12 000 7000 0.\n\nProtein structure are explained by their very diverse properties. They carry different solvability: soluble in water, some other snub solutions of immaterial salts, and some do not stimulate the retention of solubility (e.g., proteins, epithelial tissue). When fade out in water, proteins create a kind of molecular distribution system (solution of high substance). many proteins can be separate as crystals (egg protein, hemoglobin).\n\nProteins play an important role in the life of all organisms. When the protein diges tion of the molecule are digested into amino acids, which, organism well-soluble in aqueous media to disseminate into the blood stream and take down all tissues and cells. here the superlative part of amino acids consumed on protein entailment in various organs and tissues, chastna deduction of hormones, enzymes and other biologically important substances, and the residue help oneself as an energetic material. Ie acting catalytic proteins (enzymes), regulators (hormones), carry-over (hemoglobin, ceruloplasmin, etc.), rampart (antibody, thrombin, etc.)