Literature DB >> 2627305

Specificity of the binding of fd gene 5 protein to polydeoxyribonucleotides.

B C Sang1, D M Gray.   

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.

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Year:  1989        PMID: 2627305     DOI: 10.1080/07391102.1989.10508514

Source DB:  PubMed          Journal:  J Biomol Struct Dyn        ISSN: 0739-1102


  3 in total

1.  The high binding affinity of phosphorothioate-modified oligomers for Ff gene 5 protein is moderated by the addition of C-5 propyne or 2'-O-methyl modifications.

Authors:  Tung-Chung Mou; Donald M Gray
Journal:  Nucleic Acids Res       Date:  2002-02-01       Impact factor: 16.971

2.  Electrostatic potential distribution of the gene V protein from Ff phage facilitates cooperative DNA binding: a model of the GVP-ssDNA complex.

Authors:  Y Guan; H Zhang; A H Wang
Journal:  Protein Sci       Date:  1995-02       Impact factor: 6.725

3.  The binding affinity of Ff gene 5 protein depends on the nearest-neighbor composition of the ssDNA substrate.

Authors:  T C Mou; C W Gray; D M Gray
Journal:  Biophys J       Date:  1999-03       Impact factor: 4.033

  3 in total

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