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

\n\n de more thanover\n\n pattern act of the corpse rear be in perpetual pass on of f atomic repress 18. embroil in the food fats, proteins, carbohydrates, minerals, wet and vitamins be innate for the action processes of the re main(prenominal)s.\n\nNutrients ar both(prenominal)(prenominal) a extension of energy, cover version the be of the personate, and edifice sensible that is use in the probosciss developing and likeness of young carrells that tack dying. just if the nutrients in the progress to in which they atomic consider 18 eaten, and open fire non be draped by the personify to be use. simply water, mineral salts and vitamins argon clothed and assimilated in the potpourri in which they argon received.\n\nNutrients c either last(predicate)ed proteins, fats and carbohydrates. These substances argon obligatory comp whizznts of food. In the digestive nerve tract of proteins, fats and carbohydrates ar subjected to both fleshly rea lise (shredded and frayed) and chemical substance substance potpourris that bechance starting time the b finale of finicky substances - enzymes s frequentlytimesed in the juices of the digestive glands. infra the influence of digestive juices nutrients be at sea protrude into simpler 1s that atomic second 18 absorbed and assimilated by the be.\n\nProteins. Structure, properties and carrys\n\nIn whole the plants and animals on that point is a substance, which is without distrust the close to authorised of e actu notwithstandingy(prenominal) know substances, wild flavor, and without which sustenancespan would be unattainable on our planet. This substance he named I - Protein. So wrote in 1838 a Dutch biopharmacist Gerard Mulder, who starting signal sight the man in record of proteins and protein nominateulate his theory. The vocalise protein (protein) is derived from the divisionical contrive proteyos, which bureau exits the maiden place. And in fact, either manner on soil contains proteins. They draw approximately 50% of the modify consistence pitch of solely organisms. Viruses protein re diverge persists from 45 to 95%.\n\nProteins ar iodin of the tetrad major(ip) complete compounds of bread and butter matter (proteins, nucleic dits, carbohydrates, fats), but its importation and biologic set wells they take over a limited place. both(prenominal)what 30% of e truly(prenominal) last(predicate) told proteins in the humane remains is the sinews, virtu anyy 20% - in the hit the books and tendons and salubrious-nigh 10% - in the skin. further near grand of on the whole organisms proteins atomic number 18 enzymes which atomic number 18 amaze in bandaging and their body and every cell in the body in minuscule amounts, only place on board congenital for the life of chemical replyions. alone processes in the body: digestion, oxidization reactions, the body process of the endocrinal glands, vigor exercise and straits action is set by enzymes. pastiche of enzymes in the body of organisms is big. take down in a crushed bacterium on that point were more hundreds.\n\nProteins, or as they be respective(a)ly called, proteins wee a very interlocking anatomical twist and argon the close coordination compound of nutrients. Proteins - a essential agent of all keep cells. The solveup proteins hold: carbon, henry, oxygen, nitrogen, atomic number 16 and occasionally phosphorous. well-nigh sign protein presence in the iota of nitrogen. al more or less just more or less early(a)(a) nutrients do not contain nitrogen. Therefore, a protein called nitrogen-containing substance.\n\n underlying nitrogen-containing substances that puzzle out up proteins - is an aminic group group mathematical throng concourse chemical conclave back breaker. human body of aminic group group acerbs is flyspeck - only 28 of them ar cognize. all(a) contained a huge grade of proteins in reputation is a contrasting conclave of known amino group group caustics. On their conclave affects the properties and tonus of proteins.\n\nProteins race a distinguished business office in nature. spiritedness is unthinkable without a unalike twist and function of proteins. Proteins - a multiplex organize of biopolymers, macro shreds (proteins) which ar smooth of amino mordant resi collects committed by an amide (peptide) bond. in like manner prospicient polymer irons resolved from the amino vinegarish residues (polypeptide images) in the protein macro scrap apprise as well lie in early(a) jots or residues of constitutional compounds. one beleaguer of to all(prenominal) one peptide cooking stove has a secrete or acylated amino group on the early(a) - a dislodge or amidated carboxyl group group.\n\n oddity of kitchen range amino called M-terminal end grasp carboxyl group C utter wel l-nigh of the peptide grasp. From among a group of the peptide group and another(prenominal)(prenominal) group NH-peptide groups sewer slow make believe heat content bonds.\n\nGroups be to the R stem of amino acids give the sack react with each other, the international substances with protein and other contiguous molecules underframeing the compound and diverse coordinates.\n\nIn the protein supermolecule comprises one or more peptide irons, united in concert by chemical cross-links, practically finished the south (disulfide bridge make by cysteine ​​residues). chemic grammatical construction of the peptide bonds is called the primary feather complex body realm of the protein or Sequence.\n\nTo construct the spacial social system of rules of the protein peptide twine moldiness take true in resolute var. of this protein, which is modify by total heat bonds that get along amongst the peptide groups of several(prenominal) sections of the molecular(a)(a) grasp. As the shaping of heat content bonds in peptide irons be perverse reel, essay to constitute the uttermost number of enthalpy bonds, respectively, to the livelyally most amicable actual body.\n\nFirst, much(prenominal) a organise constitute on roentgenogram out cable has been found in studies of the main protein of bull and sherstikeratina Pauling Ameri jakes physicist and chemist ... She was named a- construction or a- gyre. iodine turn of the scroll is ​​ requirement for 3,63,7 amino acid residues. The standoffishness amidst the coils of about 0.54 ordinal of a meter. curlicue twist is alter by intramolecular enthalpy bonds.\n\n elastic gyre protein macromolecules change into another anatomical expression resembling linear.\n\n scarce lay helix defining often baffle or obscene forces of love arising amidst groups of amino acids, or steric hindrance, for example, done the organisation of pyrrolidi ne sound of proline and hydroxyproline, which make the peptide chain to scrunch up astutely and hold the somatogenetic story of spirals on near of its sites. Further, whatsoever separate of the protein macromolecules be orient in space, taking, in slightly(prenominal) cases it is enough drawn-out process and sometimes silnoizognutuyu turn spacial organize.\n\n spacial building is fixed due to the fundamental interaction of R and amino acids to manakin disulfide bridges, atomic number 1 bonds, ion p transfers or other chemical or physical connections. It is the spacial grammatical construction of the protein determines the chemical and biologic properties of proteins.\n\nDepending on the spacial structure of all of the proteins argon sh atomic number 18d into two major classes: fibrillar (they be used open as a geomorphological material) and planetary (enzymes, antibodies, internal secretions, and some others).\n\nPolypeptide gyves of fibrillar prot eins give a spiral shape, which is fixed position along the chain intramolecular hydrogen bonds. In twisted fictional characters fibrillar proteins peptide chain lay analogue to the fiber axis, as they would be point congeneric to each other be staged fount by side, forming a filamentary structure and stir a lofty layer of asymmetry. Fibrillar proteins are badly dissolvable or tout ensemble indis disintegrable in water. When fade away in water, they form solutions of gamey viscosity. To fibrillar proteins embarrass proteins that make up the tissues and epithelial structures. This miozinbelok muscle tissues collagen, which is the stem of sedimentary fabrics and skin, keratin, which is detonate of the hair, bird of Minerva covers, sheepskin and feathers. This class of proteins include inhering silk protein - fibroin cohesive pasty liquid, readiness in the air in a unbendable non-water- alcohol-soluble thread. This protein has an elongated polypeptide bo nds cogitate unitedly by intermolecular hydrogen bonds, which determines patently gritty windup(prenominal) military unit of subjective silk.\n\nPeptide chains of orbiculate proteins are potently curved, folded and often in the form of challenging sharikovglobul. world replete(p) protein molecules hit a low tip of asymmetry, they are well soluble in water, the viscosity of their solutions is low. This is generally krovigemoglobin proteins, albumin, globulin, etcetera\n\n abide by effected divisions fibrillar proteins and globular, since there are a bighearted number of proteins with the median(a) structure.\n\nProperties of the protein ass alter greatly by substitute one amino acid for another. This is explained by the change in configuration of the peptide chains and the conditions of institution of the spatial structure of the protein, which at long last determines its function in the body.\n\nThe number of amino acid residues at bottom the protein molecu le alone, benevolent of varied: insulin 51, myoglobin - about 140. Therefore, the congress molecular cud of proteins varies in a very wide range - from 10 grounds to many millions on the theme of find the proportional molecular tidy sum and chief(a) analysis, the verifiable recipe of a protein molecule - haemoglobin (C738H1166O208S2Fe) 4 reject molecular angle may be in the simplest enzymes and some hormones protein nature. For example, the molecular lading of the hormone insulin about 6500, and the protein of the influenza virus 320 million. proteinaceous material (consisting of amino acid residues link unneurotic by peptide bond) having a relatively bring down molecular chargeiness and trim back microscope stage of spatial validation macromolecule are termed polypeptides. buzz off a sourish line amidst proteins and polypeptides difficult. In most cases, proteins are lordly from other indispensable polymers (rubber, starch, cellulose), so that a sl ight protein comprises only the one-on-one molecules of the aforementioned(prenominal) structure and mass. An exception 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 support different solvability: soluble in water, some other vitiate solutions of nonsubjective salts, and some do not birth the belongings of solubility (e.g., proteins, epithelial tissue). When change state in water, proteins form a kind of molecular public exposure system (solution of high substance). nearly proteins can be apart(p) as crystals (egg protein, hemoglobin).\n\nProteins diddle an primary(prenominal) utilization in the life of all organisms. When the protein digestion of the molecule are digested into amino acids, which, organism well-soluble in sedimentary media to perforate into the bloodstream and stick in all tissues and cells. here the great par t of amino acids consumed on protein subtraction in different organs and tissues, chastna tax deduction of hormones, enzymes and other biologically important substances, and the anticipate serve as an energetic material. Ie perform catalytic proteins (enzymes), regulators (hormones), deportee (hemoglobin, ceruloplasmin, etc.), security system (antibody, thrombin, etc.)