Specific binding ofo-phenanthroline at a DNA structural lesion

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Specific binding of o-phenanthroline at a DNA structural lesion.

DNA intercalators are found to recognize a DNA lesion as a high affinity receptor site. This lesion-specific binding is observed when one strand of a DNA double helix contains an extra, unpaired nucleotide. Our assay for binding controls for the effects of sequence with a series of oligodeoxynucleotide duplexes which are identical except for the location of the lesion, an extra cytidine. Scissi...

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A spectroscopic study on Calf thymus DNA binding properties of nickel (II) complex with imidazole derivatives of 1,10-phenanthroline ligand

In this study, a nickel (II) complex with 1,10-phenanthroline based ligand, [Ni(FIP)2](OAC)2 (1) with FIP = 2-(Furan-2-yl)-1H-Imidazole[4,5-f][1,10] phenanthroline as ligand was synthesized and characterized by spectroscopic methods and elemental analysis. The interaction of [Ni(FIP)2](OAC)2 (1) with calf-thymus DNA (ct-DNA) was studied by UV-vis absorption, fluorescence spectroscopies and visc...

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Structural and thermodynamic strategies for site-specific DNA binding proteins.

BACKGROUND Site-specific protein-DNA complexes vary greatly in structural properties and in the thermodynamic strategy for achieving an appropriate binding free energy. A better understanding of the structural and energetic engineering principles might lead to rational methods for modification or design of such proteins. RESULTS A novel analysis of ten site-specific protein-DNA complexes reve...

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Binding experiments with alkyl-transfer-active and -inactive mutants of human O(6)-alkylguanine DNA alkyltransferase (AGT) show that it forms an O(6)-methylguanine (6mG)-specific complex on duplex DNA that is distinct from non-specific assemblies previously studied. Specific complexes with duplex DNA have a 2:1 stoichiometry that is formed without accumulation of a 1:1 intermediate. This establ...

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ژورنال

عنوان ژورنال: Nucleic Acids Research

سال: 1988

ISSN: 0305-1048,1362-4962

DOI: 10.1093/nar/16.24.11607