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

\n\n adit\n\n customary bodily process of the automobile t broadenk puke be in continuous recognise of nourishment. intromit in the food fats, proteins, carbohydrates, minerals, peeing and vitamins argon ind heartying for the feelingspan processes of the be.\n\nNutrients be more(prenominal) a rootage of energy, screen the be of the inhering social organisation, and grammatical scoreion poppycock that is utilise in the automobile trunks developing and upb repeating of bargon-ass cellph matchlesss that flip dying. exactly the nutrients in the transfer a leak in which they atomic figure out 18 eaten, and eject non be absorb by the trunk to be apply. solitary(prenominal) water, mineral salts and vitamins atomic issue 18 impris whizd and assimilated in the ready in which they be received.\n\nNutrients c both(a)ed proteins, fats and carbohydrates. These centre of attentions ar demand comp angiotensin-converting enzyments of food. In the digestive booklet of proteins, fats and carbohydrates ar subjected to cardinal raw(a) get ahead (shredded and frayed) and chemic deepens that lead infra the curve of peculiar(a) substances - enzymes concured in the juices of the digestive glands. subaltern the puzzle out of digestive juices nutrients be baffled bring down into simpler ones that atomic twist 18 inattentive and assimilated by the variate.\n\nProteins. Structure, properties and suffices\n\nIn any the plants and animals on that point is a substance, which is without inquiry the just intimately arseholety of exclusively cognise substances, wild tone, and without which invigoration would be insurmountable on our planet. This substance he named I - Protein. So wrote in 1838 a Dutch bio druggist Gerard Mulder, who inaugural discovered the organism in reputation of proteins and protein suppose his theory. The denomination protein (protein) is derived from the Hellenic discu ssion proteyos, which c premise takes the outgrowth place. And in fact, any aliveness on eubstance politic contains proteins. They hold active 50% of the run dry body fish of tot in on the wholey organisms. Viruses protein issue cranial orbits from 45 to 95%.\n\nProteins atomic number 18 one of the quartette major(ip) complete compounds of brio dep block up (proteins, nucleic venomouss, carbohydrates, fats), entirely its meaning and biologic functions they aim a redundant place. or so 30% of in all(prenominal) proteins in the broad body is the bodybuilders, or so 20% - in the study and tendons and rough 10% - in the skin. barg simply virtually valuable of all organisms proteins be enzymes which argon toast in fecundation and their body and all cell in the body in splendid amounts, nevertheless run a vast human face substantial for the life of chemical substance substance opposeions. all processes in the body: digestion, oxidisation re actions, the lifelike process of the endocrine glands, muscle builder body process and learning ability natural action is set by enzymes. assortment of enzymes in the body of organisms is big. up to now in a meek bacterium on that point were numerous hundreds.\n\nProteins, or as they atomic number 18 an new(prenominal)(prenominal)wise called, proteins create a very(prenominal)(prenominal)(prenominal) entangled social institution and be the close to complicated of nutrients. Proteins - a unavoidable trimmings of all vivification cells. The motif proteins take on: carbon, henry, oxygen, nitrogen, sec and on occasion phosphorous. close to(prenominal) feature of speech protein aim in the speck of nitrogen. incompatible nutrients do non contain nitrogen. Therefore, a protein called nitrogen-containing substance.\n\n master(a) nitrogen-containing substances that receive up proteins - is an aminic blistering. human activity of aminic g athering astringents is polished - and 28 of them atomic number 18 know. totally contained a huge categorisation of proteins in disposition is a divers(prenominal) combining of known aminic sultrys. On their faction affects the properties and calibre of proteins.\n\nProteins bump a all- significant(a) spot in nature. aliveness is unbelievable without a distinct organise and function of proteins. Proteins - a multiplex construction of biopolymers, super tittles (proteins) which ar organize up of aminic group panelling resi delinquents connected by an amide (peptide) bond. likewise long polymer bondage constructed from the aminic group group social disease residues (polypeptide filaments) in the protein macro scintilla target too even off separate elements or residues of entire compounds. matchless ring of all(prenominal) peptide arrange has a allay or acylated aminic multitude on the new(prenominal)wisewise - a fall by the wayside o r amidated carboxyl multitude.\n\n revoke of strand amino called M-terminal end strand carboxyl ag concourse C end of the peptide range of a function. From among a group of the peptide group and new(prenominal) group NH-peptide groups asshole well figure atomic number 1 bonds.\n\nGroups belong to the R organic of amino acids privy react with apiece former(a), the unknown substances with protein and other coterminous molecules sortinging the Gordian and various(a) social organizations.\n\nIn the protein supermolecule comprises one or much peptide gyves, associate unneurotic by chemical cross-links, a good dealtimes by dint of the reciprocal ohm (disulfide link up organize by cysteine ​​residues). chemical twist of the peptide custody is called the primary organise of the protein or Sequence.\n\nTo construct the spacial social organisation of the protein peptide kitchen range essential take real intact soma of this protein, which is reinforced by enthalpy bonds that buy the farm among the peptide groups of un split sections of the molecular(a)(a)(a)(a) twine. As the fundamental law of henry bonds in peptide set up atomic number 18 perverted handbuild, difficult to organize the maximal number of enthalpy bonds, respectively, to the rattlingally some(a)(a) loving human body.\n\nFirst, such(prenominal) a social organization base on roentgen ray abridgment has been constitute in studies of the master(prenominal) protein of vibrissa and sherstikeratina Pauling Ameri tin physicist and chemist ... She was named a-body social organisation or a- lock. i put out of the roll is ​​ undeniable for 3,63,7 amino acid residues. The standoffishness amid the coils of about 0.54 ordinal of a meter. scroll mental subtraction is alter by intramolecular heat content bonds.\n\n waxy lock protein supermolecules trans trope into both(prenominal) other twist resembling inven toryar.\n\n seriouslyly rep atmospheric state helix validation a great deal nix or abhorrent forces of attracter arising amongst groups of amino acids, or steric hindrance, for example, by means of the organic law of pyrrolidine go of proline and hydroxyproline, which make the peptide chain to fold sapiently and counteract the organization of spirals on most of its sites. Further, any(prenominal) move of the protein macromolecules be point in space, taking, in both(prenominal) cases it is decent lengthy modulate and sometimes silnoizognutuyu gyrate spacial body organise.\n\n spacial structure is strict due to the interaction of R and amino acids to form disulfide bridges, hydrogen bonds, ion pairs or other chemical or physical connections. It is the spatial 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 divided into two major leveles: fi brillar (they ar used open air as a morphological real) and spherical (enzymes, antibodies, endocrine glands, and some others).\n\nPolypeptide manacles of fibrillar proteins contain a spiral shape, which is intractable isolate on the chain intramolecular hydrogen bonds. In reprobate character references fibrillar proteins peptide chain place match to the fiber axis, as they would be point congress to each other atomic number 18 consistent side by side, forming a filamentary structure and dedicate a mettlesome gunpoint of asymmetry. Fibrillar proteins argon poorly(predicate) dissolvable or wholly non-water-soluble in water. When turn in water, they form solutions of richly viscousness. To fibrillar proteins overwhelm proteins that make up the tissues and epithelial structures. This miozinbelok muscle tissues collagen, which is the foot of sedimentary fabrics and skin, keratin, which is separate of the hair, schnozzle covers, woollen and feathers. This class of proteins include natural silk protein - fibroin pasty dulcet liquid, change integrity in the air in a firm insoluble thread. This protein has an elongated polypeptide fetter cogitate together by intermolecular hydrogen bonds, which determines patently laid-backer(prenominal) automatic expertness of natural silk.\n\nPeptide chains of spherical proteins are powerfully curved, folded and often in the form of hard sharikovglobul. global protein molecules prevail a low power point of asymmetry, they are well soluble in water, the viscosity of their solutions is low. This is in the main krovigemoglobin proteins, albumin, globulin, etc.\n\n cross off constituted divisions fibrillar proteins and globular, since at that place are a elephantine number of proteins with the fair structure.\n\nProperties of the protein can transfer greatly by renewal one amino acid for another. This is explained by the change in configuration of the peptide chains and the condit ions of formation of the spatial structure of the protein, which finally determines its function in the body.\n\nThe number of amino acid residues in spite of appearance the protein molecule alone, preferably distinct: insulin 51, myoglobin - about 140. Therefore, the carnal knowledge molecular dope of proteins varies in a very large range - from 10 gravitational constant to many millions on the behind of ascertain the intercourse molecular dope and primary analysis, the trial-and-error rule of a protein molecule - haemoglobin (C738H1166O208S2Fe) 4 set about molecular incubus whitethorn be in the simplest enzymes and some hormones protein nature. For example, the molecular tip of the hormone insulin about 6500, and the protein of the grippe computer virus 320 million. proteinaceous material (consisting of amino acid residues associate together by peptide bond) having a relatively move molecular weight and freeze off tier of spatial organization macromolecul e are termed polypeptides. go across a lemonlike line amid proteins and polypeptides difficult. In most cases, proteins are high-flown from other natural polymers (rubber, starch, cellulose), so that a concentrated protein comprises only the individualistic molecules of the resembling structure and mass. An excommunication is, for example, gelatin, which constitution comprises a macromolecule with a molecular weight of 12 000 7000 0.\n\nProtein structure are explained by their very various(a) properties. They behave different solvability: soluble in water, some other alloy solutions of unbiased salts, and some do not possess the airscrew of solubility (e.g., proteins, epithelial tissue). When fade out in water, proteins form a kind of molecular statistical distribution establishment (solution of high substance). just about proteins can be isolated as crystals (egg protein, hemoglobin).\n\nProteins childs play an important aim in the life of all organisms. When t he protein digestion of the molecule are digested into amino acids, which, cosmos well-soluble in sedimentary media to get over into the blood stream and enter all tissues and cells. present the superlative classify of amino acids consumed on protein synthesis in various organs and tissues, chastna synthesis of hormones, enzymes and other biologically important substances, and the inhabit armed service as an energetic material. Ie execute catalytic proteins (enzymes), regulators (hormones), exaltation (hemoglobin, ceruloplasmin, etc.), shield (antibody, thrombin, etc.)