title: Specificity of the binding of fd gene 5 protein to polydeoxyribonucleotides.
abstract: The long-wavelength circular dichroism (CD) changes induced by binding of fd gene 5 protein to the alternating DNA sequences poly[d(A-C)] and poly[d(C-T)] were similar to those induced by the protein complexed with the homopolymers poly[d(A)], poly[d(C)], and poly[d(T)]. The fd gene 5 protein showed different binding affinities for the various polymers. The affinity for the alternating sequences was not compositionally weighted with respect to the affinities for the homopolymers, indicating that both base composition and base sequence of the template are important for the binding of fd gene 5 protein.
authors.affiliation: Program in Molecular and Cell Biology, University of Texas at Dallas, Richardson 75083-0688.
authors.forename: B C
authors.initials: BC
authors.lastname: Sang
authors.forename: D M
authors.initials: DM
authors.lastname: Gray
mesh_terms: D001435:Bacteriophages / Q000235:genetics; D002942:Circular Dichroism; D004247:DNA / Q000187:drug effects*; D004268:DNA-Binding Proteins / Q000378:metabolism* / Q000493:pharmacokinetics*; D011089:Polydeoxyribonucleotides / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D004268:DNA-Binding Proteins; D011089:Polydeoxyribonucleotides; D014764:Viral Proteins; C057816:gene 5 protein, Enterobacteria phage M13; D004247:DNA