Cooperativity in binding of proteins to DNA

A. Ben-Naim*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Three different, linear, three-site binding models are presented for the binding of proteins, such as a repressor, to DNA. The first model assumes that the DNA is rigid and all correlations between the ligands are due to direct ligand-ligand interactions. In the second and third models conformational changes in the DNA are induced by the binding process. In these models we find both direct and indirect correlations between the ligands. Examination of the indirect correlation reveals two characteristic features that, in general, are negligible in the direct correlation. (1) Long range correlation, between nonadjacent sites. (2) Nonadditivity of the triplet correlations. It is shown that these two features cannot be neglected in the indirect correlations. The arguments for explaining these features are similar to those which explain long range and nonadditivies of correlations in the liquid state.

Original languageEnglish
Pages (from-to)10242-10252
Number of pages11
JournalJournal of Chemical Physics
Volume107
Issue number23
DOIs
StatePublished - 15 Dec 1997

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