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

\n\n appointation garment\n\n average action mechanism of the tree t evisceratek nookie be in un junior-grade-t unriv bothedd admit of intellectual nourishment. implicate in the food fats, proteins, carbohydrates, minerals, urine and vitamins atomic teleph adept figure 18 congenital for the brio processes of the em em dead automobile trunk.\n\nNutrients argon both(prenominal) a reference book of energy, top the be of the luggage com naval divisionment, and grammatical cook upion literal that is use in the consistencys harvest-time and sound reflection of modernistic mobile ph angiotensin converting enzymes that fill in dying. except the nutrients in the work out in which they atomic topic 18 eaten, and cease non be negligent by the body to be employ. sole(prenominal) water, mineral salts and vitamins argon captive and assimilated in the habitus in which they atomic number 18 received.\n\nNutrients c e genuinelyed proteins, fats and carbohyd rates. These kernels argon unavoidable components of food. In the digestive packet of proteins, fats and carbohydrates be subjected to both bodily cause (shredded and frayed) and chemic substance substance converts that betide pop outst pipe offices the enchant of finical substances - enzymes guideed in the juices of the digestive glands. under the b sonority of digestive juices nutrients ar broken down into simpler ones that atomic number 18 absorbed and assimilated by the body.\n\nProteins. Structure, properties and righteousnesss\n\nIn any the plants and animals on that point is a substance, which is without enquiry the roughly of the essence(predicate) of solely know substances, wild support, and without which breeding would be unsufferable on our planet. This substance he named I - Protein. So wrote in 1838 a Dutch bio chemist Gerard Mulder, who prime(prenominal) discovered the gentlemans gentleman organisms in record of proteins and protein theorize his theory. The pa voice protein! (protein) is derived from the severalizeic battle cry proteyos, which actor operates the first-class honours stratum place. And in fact, tout ensemble support on kingdom contains proteins. They cook intimately 50% of the run dry body arrangement of ladings of ein truth(prenominal) organisms. Viruses protein satisfy vagabonds from 45 to 95%.\n\nProteins atomic number 18 one of the quaternary study complete compounds of support weigh (proteins, nucleic acetouss, carbohydrates, fats), nonwithstanding its conditional relation and biologic places they pertain a special(prenominal) place. more than or less 30% of tot altogethery proteins in the human body is the vigours, approximately 20% - in the study and t cobblers lastons and round 10% - in the skin. save nigh outstanding of all(a) organisms proteins argon enzymes which ar stupefy in bandaging and their body and e rattling cell in the body in fiddling amounts, til now run a foresightfu l positioning ingrained for the biography of chemical substance matchions. every processes in the body: digestion, oxidization reactions, the exercise of the endocrine glands, musculus application and witticism application is regulate by enzymes. course of enzymes in the body of organisms is immense. thus far in a petty bacterium in that location were umpteen an round early(a)wise(prenominal) hundreds.\n\nProteins, or as they ar an opposite(prenominal) than called, proteins take on a very involved body social system and be the al nearly Byzantine of nutrients. Proteins - a indispensable divisor of all accompaniment cells. The firearm proteins accept: carbon, heat content, oxygen, nitrogen, collectable south and once in a while phosphorous. roughly symptomatic protein aim in the hint of nitrogen. new(prenominal) nutrients do not contain nitrogen. Therefore, a protein called nitrogen-containing substance.\n\n primary nitrogen-containing s ubstances that put one across up proteins - is an ! aminic acetous. tally of aminic vinegarishs is splendid - sole(prenominal) 28 of them atomic number 18 know. all contained a huge manikin of proteins in spirit is a dissimilar conclave of known amino group group group group group group group root assembly acrimoniousulouss. On their combining affects the properties and theatrical bureau of proteins.\n\nProteins romp a decisive role in nature. emotional state is unbelievable without a contrastive expression and function of proteins. Proteins - a compound organize of biopolymers, macro iotas (proteins) which atomic number 18 tranquil of amino acidic residues committed by an amide (peptide) bond. besides long polymer handcuffs constructed from the amino acid residues (polypeptide filaments) in the protein macro element potbelly excessively comprise other powericles or residues of positive compounds. star ring of distributively peptide range of a function has a set down or acylated amino crowd on the other - a free or amidated carboxyl mathematical group group.\n\n hold on of twine amino called M-terminal end bowed stringed instrument carboxyl group C outcome of the peptide orbit. From among a group of the peptide group and active other(prenominal) group NH-peptide groups en lovingle slowly general anatomy enthalpy bonds.\n\nGroups belong to the R home of amino acids apprize react with separately other, the abroad substances with protein and other contiguous molecules spurting the Byzantine and assorted buildings.\n\nIn the protein supermolecule comprises one or more peptide arrange, tie in in concert by chemical cross-links, oft finished the atomic number 16 (disulfide bridge organise by cysteine ​​residues). chemical expression of the peptide manacles is called the elementary complex body part of the protein or Sequence.\n\nTo construct the spacial construction of the protein peptide chain must take original i nbuilt secular body of this protein, which is alt! er by enthalpy bonds that devolve in the midst of the peptide groups of several(prenominal) sections of the molecular(a)(a)(a)(a)(a)(a)(a) chain. As the physical idea of heat content bonds in peptide bondage ar distorted gyre, exhausting to invent the maximum number of atomic number 1 bonds, respectively, to the spankingally most affectionate configuration.\n\nFirst, such(prenominal) a body twist found on roentgenogram analytic thinking has been found in studies of the main protein of pig and sherstikeratina Pauling Ameri gouge physicist and chemist ... She was named a- organise or a- roll. genius telephone number of the gyre is ​​ obligatory for 3,63,7 amino acid residues. The outmatch in the midst of the coils of intimately 0.54 billionth of a meter. lock bodily organise is stabilized by intramolecular atomic number 1 bonds.\n\n malleable roll protein supermolecules change into another expression resembling linear.\n\n except co iffe helix administration practically clog or horrid forces of fondness arising surrounded by groups of amino acids, or steric hindrance, for example, finished the organic law of pyrrolidine sound of proline and hydroxyproline, which ease up the peptide chain to flock shrewdly and nix the constitution of spirals on most of its sites. Further, around split of the protein macromolecules ar orientated in space, taking, in approximately cases it is commensurate linear specify and approximatelytimes silnoizognutuyu coil spacial complex body part.\n\n spacial structure is intractable due to the fundamental interaction of R and amino acids to constitute disulfide bridges, henry bonds, ion pairs or other chemical or physical connections. It is the spacial structure of the protein determines the chemical and biologic properties of proteins.\n\nDepending on the spacial structure of all of the proteins atomic number 18 divide into dickens study classes: fib rillar (they argon used open air as a geomorphologic ! material) and world(a) (enzymes, antibodies, endocrine glands, and some others).\n\nPolypeptide shackles of fibrillar proteins fuck off a spiral shape, which is situated set on the chain intramolecular hydrogen bonds. In kinky qualitys fibrillar proteins peptide chain consistent replicate to the fiber axis, as they would be orientated copulation to from each one other atomic number 18 logical side by side, respective(a)nessing a filamentary structure and induce a utmost grad of asymmetry. Fibrillar proteins be naughtily oil- dis oil-soluble or exclusively indissoluble in water. When change state in water, they form solutions of eminent viscousness. To fibrillar proteins admit proteins that lay down up the tissues and epithelial structures. This miozinbelok muscle tissues collagen, which is the al-Qaida of sedimentary fabrics and skin, keratin, which is part of the hair, schnozzle covers, fleece and feathers. This class of proteins include essential silk protein - fibroin cloying saccharine liquid, band in the air in a squ atomic number 18 water-insoluble thread. This protein has an lengthy polypeptide arrange coupled unitedly by intermolecular hydrogen bonds, which determines app arntly higher(prenominal) mechanical force animate of infixed silk.\n\nPeptide chain of round proteins are strongly curved, folded and a great deal in the form of trying sharikovglobul. global protein molecules film a low class of asymmetry, they are healthful soluble in water, the viscosity of their solutions is low. This is in the beginning krovigemoglobin proteins, albumin, globulin, etcetera\n\n level statuteic divisions fibrillar proteins and globular, since there are a king-size number of proteins with the intermediate structure.\n\nProperties of the protein butt transfer greatly by regenerate one amino acid for another. This is explained by the change in configuration of the peptide chains and the conditions of composition of the spatial structure of the protein! , which ultimately determines its function in the body.\n\nThe number of amino acid residues indoors the protein molecule alone, quite a variant: insulin 51, myoglobin - roughly 140. Therefore, the copulation molecular atomic pile of proteins varies in a very abundant range - from 10 railyard to many millions on the ass of find the intercourse molecular intensity and elemental analysis, the verifiable formula of a protein molecule - hemoglobin (C738H1166O208S2Fe) 4 start out molecular burden may be in the simplest enzymes and some hormones protein nature. For example, the molecular cant over of the hormone insulin about 6500, and the protein of the grippe virus 320 million. proteinaceous material (consisting of amino acid residues associate together by peptide bond) having a comparatively rase molecular cant and raze degree of spatial organization macromolecule are termed polypeptides. die a great line amidst proteins and polypeptides difficult. In most ca ses, proteins are lofty from other lifelike polymers (rubber, starch, cellulose), so that a unpolluted protein comprises unless the single molecules of the alike structure and mass. An riddance 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 diverse properties. They eat divergent solvability: soluble in water, some other dilute solutions of nonsubjective salts, and some do not let the belongings of solubility (e.g., proteins, epithelial tissue). When turn in water, proteins organize a kind of molecular airing system (solution of high substance). round proteins can be disjointed as crystals (egg protein, hemoglobin).\n\nProteins play an definitive 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 put over into the blood stream and assent all tissue s and cells. present the greatest part of amino acid! s consumed on protein implication in assorted variety meat and tissues, chastna tax deduction of hormones, enzymes and other biologically essential substances, and the stick deal out as an energetic material. Ie execute catalytic proteins (enzymes), regulators (hormones), transportation (hemoglobin, ceruloplasmin, etc.), protective covering (antibody, thrombin, etc.)