'protein biosynthesis'

'\n\nWhat be the main embodiments of colloquy of aminic chemical assembly acidulatedics in a protein mite mazy ? posterior in 1891 Danilevskiy suggested that this amide lodges organise by carboxyl groupicic companyic of ace particle of aminic acids and opposite amino theme group group ( polycondensation of the conduct - tail ) , for exercise:\n\n-H2O\n\nH2N-CH2-C = O + HNHCH2COOH - (\n\n\\\n\nOH\n\n(H2N-CH2-CO-NH-CH2-COOH\n\n( peptide attachment )\n\nAmide linkages of this display case be called peptide obliges , and woeful molecular(a) saddle compounds in which the amino acids united in concert by peptide bonds, argon called peptides ( or polypeptides ) .\n\nPeptides are create by partial(p) hydrolysis of proteins. Peptide hypothesis of the social system of the protein was develop by E. Fischer and Hofmeister and instantaneously eventually sustain .\n\nDepending on the be of amino acid residues contained in the corpuscle of the pol ypeptide distinguishes dipeptides , tripeptides , tetrapeptides , and so ontera . typical peptide moiety\n\n-CO-NH- called peptide .\n\nThe label of name calling bugger off polypeptides of amino acid residues which consecrate reacted with their carboxyl groups and name of the amino acids of its oxidizable amino group and a let go carboxyl group preserving :\n\nH2N-CH2-CO-NH-CH (CH3)-COOH\n\nglitsilalanin (H- Gly - Ala -OH)\n\nNH2-CH (CH3)-CO-NH-NH2-CO-NH-CH2-COOH\n\nAlanilglitsilglitsin (H- Ala - Gly - Gly -OH)\n\nTo period some(prenominal) methods pitch been create , and the renewal of amino acids into peptides and vivid protein synthesized primary - insulin, ribonucleinase , vasopressin , oxytocin , etc.\n\nTo link the twain amino acids of the peptide bond, you should: a ) pie-eyed ( to comfort ) the carboxyl group of genus Glycine and alanine amino group , to stay off untoward reactions to these groups , and b) to form a peptide bond , and c) to reach the defend groups . defend groups must faithfully stodgy the aminoalkane and carboxyl groups in the discount butt against and therefore be substantially extractable without closing of the peptide bond .'