Energetics of the Escherichia coli DnaT protein trimerization reaction.

Abstract

Thermodynamic and structural characteristics of the Escherichia coli DnaT protein trimerization reaction have been quantitatively examined using fluorescence anisotropy and analytical ultracentrifugation methods. Binding of magnesium to the DnaT monomers regulates the intrinsic affinity of the DnaT trimerization reaction. Comparison between the DnaT trimer… (More)
DOI: 10.1021/bi3015696

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Cite this paper

@article{Szymanski2013EnergeticsOT, title={Energetics of the Escherichia coli DnaT protein trimerization reaction.}, author={Michal R Szymanski and Maria J. Jezewska and Wlodzimierz Bujalowski}, journal={Biochemistry}, year={2013}, volume={52 11}, pages={1858-73} }