Adenine Base Unstacking Dominates the Observed Enthalpy and Heat Capacity Changes for the Escherichia coli SSB Tetramer Binding to Single-Stranded Oligoadenylates †

Large contributions of coupled protonati

Large contributions of coupled protonation equilibria to the observed enthalpy and heat capacity changes for ssDNA binding to Escherichia coli SSB protein

✍ Alexander G. Kozlov; Timothy M. Lohman 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 342 KB 👁 2 views

Many macromolecular interactions, including protein-nucleic acid interactions, are accompanied by a substantial negative heat capacity change, the molecular origins of which have generated substantial interest. We have shown previously that temperature-dependent unstacking of the bases within oligo(