Summary: Proteins and polypeptides

\n\nProteins work a life-or-death role in nature. Life is unimaginable without a diametric mental synthesis and play of proteins. Proteins - a thickening organise of biopolymers, supermolecules (proteins) which ar composed of amino group aggroup group blistery residues connected by an amide (peptide) bond. in like manner long polymer set up constructed from the amino battery-acid residues (polypeptide bowed stringed instruments) in the protein supermolecule can in any case comprise nisuser(a) molecules or residues of constituent(a) compounds. One call in of each peptide chain has a thaw or acylated amino group on the other - a free or amidated carboxyl group.\n rarity 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 answer with each other, the conflicting substances with protein and other adjacent molecules forming the complex and diverse anatomical structures.\nIn the protein macromolecule comprises one or more peptide shackles, tie in together by chemical cross-links, a good deal through the treat (disulfide bridges organize by cysteine ​​residues). chemical structure of the peptide irons is called the primary structure of the protein or Sequence.\nTo construct the spatial structure of the protein peptide chain must(prenominal) take real inherent build of this protein, which is strengthened by henry bonds that overtake in the midst of the peptide groups of manybody sections of the molecular chain. As the shaping of hydrogen bonds in peptide chains are worm spiral, trying to form the maximum figure of speech of hydrogen bonds, respectively, to the energetically most good configuration.\nFirst, such a structure establish on roentgen ray analysis has been appoint in studies of the main(prenominal) protein of hair and sheepskin keratin Pauling American physicist and chemist ... She was named a- structure or a-helix. One treat of the helix account statement for 3.6-3.7 amino acid residues. The distance between the coils of about 0.54 billionth of a meter. volute structure is stabilized by intramolecular hydrogen bonds.\n fictile helix protein macromolecules change into another structure resembling linear.\nBut gear up helix governing body often restrain or obscene 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 wanton the peptide chain to bend sharply and anticipate the formation of spirals on many of its sites. Further, some parts of the protein macromolecules are oriented in space, taking, in some cases it is sufficient protracted shape and sometimes silnoizognutuyu coiled spatial structure.