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  • Book
    Irena Roterman, Leszek Konieczny, editors.
    Summary: This book is an open access under a CC BY license. The subject of this book relates to protein ligands with particular structural and complexation properties. They are composed of self-assembled molecules, capable of penetrating as a unit into proteins outside the binding site. The ribbon-like supramolecular system only permits the penetration of self-assembled molecules into the protein-body and formation of stable complexes. Supramolecular Congo red and similar compounds fit these requirements. Destabilized protein fragments enable the penetration of such ligands, with susceptibility to supramolecular ligand binding often associated with protein function. As a result, complexation modifies their functional effects. The activity of enzymes is inhibited by arresting them in the complexed state, but "naturally irreversible" complexation as in the case of immune complexation, is enhanced instead. This property offers many attractive possibilities of using supramolecular ligands as described in this book.

    Contents:
    Supramolecular systems as protein ligands
    Supramolecular Congo Red as Specific Ligand of Antibodies Engaged in Immune Complex
    Protein Conditioning for Binding Congo Red and Other Supramolecular Ligands
    Metal Ions Introduced to Proteins by Supramolecular Ligands
    Possible Mechanism of Amyloidogenesis of V Domains
    Supramolecular Structures as Carrier Systems Enabling the Use of Metal Ions in Antibacterial Therapy
    Congo Red Interactions with Single-Walled Carbon Nanotubes.
    Digital Access Springer 2018
  • Article
    Duncan BK, Rockstroh PA, Warner HR.
    J Bacteriol. 1978 Jun;134(3):1039-45.
    A new assay specific for uracil-DNA glycosylase is described, Escherichia coli mutants partially and totally deficient in uracil-DNA glycosylase activity have been isolated by using this assay in mass-screening procedures. These have been designated ung mutants. The ung gene maps between tyrA and nadB on the E. coli chromosome. T4 phage containing uracil in their DNA grow on the most glycosylase-deficient hosts but are unable to grow on wild-type bacteria. This provides a simple spot test for the ung genotype. The ung mutants show slightly higher rates of spontaneous mutation to antibiotic resistance. Taken together, these results suggest a central role for uracil-DNA glycosylase in the initiation of an excision repair pathway for the exclusion of uracil from DNA.
    Digital Access Access Options