Protein–DNA Interactions: Polyelectrolyte Effects

Abstract

The stability of noncovalent protein–DNA complexes is typically sensitive to the ionic composition of the solution, in a manner that is dependent on the specific ion concentrations and is not a simple ionic strength effect. One important origin of this sensitivity to solution conditions is the polyelectrolyte effect.

Keywords: Protein–nucleic acid interactions; thermodynamics; polyelectrolytes; binding

References

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Further Reading

Ballin JD, Shkel IA and Record MT Jr (2004) Interactions of the KWK6 cationic peptide with short nucleic acid oligomers: demonstration of large Coulombic end effects on binding at 0.1‐0.2 M salt. Nucleic Acids Research 32: 3271–3281.

Cayley S and Record MT Jr (2004) Large changes in cytoplasmic biopolymer concentration with osmolality indicate that macromolecular crowding may regulate protein–DNA interactions and growth rate in osmotically stressed E. coli K‐12. Journal of Molecular Recognition 17: 488–496.

Csonka LN and Epstein W (1996) Osmoregulation. In: Neidhardt FC, Curtiss R III, Ingraham JL et al. (eds) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, 2nd edn, vol. 1, pp. 1210–1223. Washington, DC: ASM Press.

Lohman TM and Mascotti DP (1992) Thermodynamics of ligand–nucleic acid interactions. Methods in Enzymology 212: 400–424.

von Hippel P (2007) From “simple” DNA‐protein interactions to the macromolecular machines of gene expression. Annual Review of Biophysics and Biomolecular Structure 36: 79–105.

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How to Cite close
Saecker, Ruth M(Sep 2007) Protein–DNA Interactions: Polyelectrolyte Effects. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0001350.pub2]