Results 1–5 of 5 for polipeptid
Polypeptides are peptides containing ten or more amino acid residues. The properties of a polypeptide are determined by the type and sequence of its constituent amino acids.
Cross-linking is an attachment of two chains of polymer molecules by bridges, composed of either an element, a group, or a compound, that join certain carbon atoms of the chains by primary chemical bonds, as indicated in the schematic diagram
Cross-linking occurs in nature in substances made up of polypeptide chains that are joined by the disulfide bonds of the cysteine residue, as in keratins or insulin. Cross-linking can be artificially effected, either adding a chemical substance (cross-linking agent), or by subjecting the polymer to high-energy radiation. Examples are: vulcanisation of rubber with sulphur, cross-linking of polystyrene with divinylbenzene, or cross-linking of polyethylene by means of high-energy radiation.
Cross-linking has the effect of changing a plastic from thermoplastic to thermosetting. Thus, it also increases strength, heat and electrical resistance, and especially resistance to solvents and other chemicals.
Deoxyribonucleic acid (DNA) is a nucleic acid with 2-deoxy-D-ribose as the sugar in its nucleotides. DNA contains encoded genetic information, specifically templates for the synthesis of all of an organism’s proteins and enzymes.
DNA was first identified in the 1869 by Swiss chemist Friedrich Miescher (1844-1895). In 1953, American biologist James Dewey Watson (1928-) and English physicist Francis Harry Compton Crick (1916–2004) had discovered that DNA occurs in the cell as a double helix, with two long strands of the molecule wound around each other, and further that the chemical structure of the molecule dictates that adenine (A) always aligns or pairs with thymine (T), and cytosine (C) always pairs with guanine (G). It is this base pairing that allows DNA in a cell to copy itself, and transfer its information to a new cell. The diameter of the helix is 2.0 nm and there is a residue on each chain every 0.34 nm in the z direction. The angle between each residue on the same strand is 36°, so that the structure repeats after 10 residues (3.4 nm) on each strand.
Proline has an aliphatic side chain with a distinctive cyclic structure. It is unusual because it is conformationally restricted. The secondary amino (imino) group of proline residues is held in a rigid conformation that reduces the structural flexibility of polypeptide regions containing proline. It is not an essential amino acid, which means that the human body can synthesize it.
Generalic, Eni. "Polipeptid." Croatian-English Chemistry Dictionary & Glossary. 29 June 2022. KTF-Split. {Date of access}. <https://glossary.periodni.com>.
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