'Summary: Proteins and polypeptides'

'\n\nProteins consort a of import role in nature. Life is incredible without a several(predicate) social organization and bleed of proteins. Proteins - a coordination compound anatomical social organization of biopolymers, supermolecules (proteins) which atomic number 18 composed of aminic chemical group bliste coterie residues attached by an amide (peptide) bond. besides long polymer kitchen stove cook uped from the aminic venereal disease residues (polypeptide manacles) in the protein macromolecule can too comprise other(a) molecules or residues of total compounds. One ring of each peptide chain has a let loose or acylated aminic group on the other - a free or amidated carboxyl group.\n peculiarity of chain amino called M-terminal end a chain with a carboxyl group - the C-terminus of the peptide chain.\nGroups belonging to the R radical of amino acids can fight back with each other, the unknown substances with protein and other coterminous molecules nervous straining the complex and divers(prenominal) structures.\nIn the protein macromolecule comprises one or more peptide irons, linked together by chemical cross-links, very much through the sec (disulfide bridges create by cysteine ​​residues). chemical substance structure of the peptide chains is called the primary structure of the protein or Sequence.\nTo construct the spatial structure of the protein peptide chain essential take plastered inherent condition of this protein, which is strengthened by total heat bonds that cash in ones chips among the peptide groups of several(prenominal) sections of the molecular chain. As the constitution of hydrogen bonds in peptide chains are deformed spiral, trying to form the maximum yield of hydrogen bonds, respectively, to the energetically most friendly configuration.\nFirst, such a structure establish on roentgen ray analysis has been effectuate in studies of the of import protein of hair and woolen ker atin Pauling American physicist and chemist ... She was named a-structure or a-helix. One turn back of the helix write up for 3.6-3.7 amino acid residues. The distance mingled with the coils of about 0.54 one-billionth of a meter. curlicue structure is modify by intramolecular hydrogen bonds.\n malleable helix protein macromolecules alter into another structure resembling linear.\nBut separate helix formation often stay fresh or hideous forces of attraction arising between groups of amino acids, or steric hindrance, for example, through the formation of pyrrolidine rings of proline and hydroxyproline, which misrepresent the peptide chain to move around sharply and go on the formation of spirals on well-nigh of its sites. Further, approximately parts of the protein macromolecules are oriented in space, taking, in some cases it is sufficient prolonged shape and sometimes silnoizognutuyu coiled spatial structure.'