{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vander Meulen KA"],"funding":["NIGMS NIH HHS"],"pagination":["9-27"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2336898"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["377(1)"],"pubmed_abstract":["To characterize driving forces and driven processes in formation of a large-interface, wrapped protein-DNA complex analogous to the nucleosome, we have investigated the thermodynamics of binding the 34-base pair (bp) H' DNA sequence to the Escherichia coli DNA-remodeling protein integration host factor (IHF). Isothermal titration calorimetry and fluorescence resonance energy transfer are applied to determine effects of salt concentration [KCl, KF, K glutamate (KGlu)] and of the excluded solute glycine betaine (GB) on the binding thermodynamics at 20 degrees C. Both the binding constant K(obs) and enthalpy Delta H degrees (obs) depend strongly on [salt] and anion identity. Formation of the wrapped complex is enthalpy driven, especially at low [salt] (e.g., Delta H(o)(obs)=-20.2 kcal x mol(-"],"journal":["Journal of molecular biology"],"pubmed_title":["Formation of a wrapped DNA-protein interface: experimental characterization and analysis of the large contributions of ions and water to the thermodynamics of binding IHF to H' DNA."],"pmcid":["PMC2336898"],"funding_grant_id":["R37 GM023467","GM 23467"],"pubmed_authors":["Vander Meulen KA","Saecker RM","Record MT"],"additional_accession":[]},"is_claimable":false,"name":"Formation of a wrapped DNA-protein interface: experimental characterization and analysis of the large contributions of ions and water to the thermodynamics of binding IHF to H' DNA.","description":"To characterize driving forces and driven processes in formation of a large-interface, wrapped protein-DNA complex analogous to the nucleosome, we have investigated the thermodynamics of binding the 34-base pair (bp) H' DNA sequence to the Escherichia coli DNA-remodeling protein integration host factor (IHF). Isothermal titration calorimetry and fluorescence resonance energy transfer are applied to determine effects of salt concentration [KCl, KF, K glutamate (KGlu)] and of the excluded solute glycine betaine (GB) on the binding thermodynamics at 20 degrees C. Both the binding constant K(obs) and enthalpy Delta H degrees (obs) depend strongly on [salt] and anion identity. Formation of the wrapped complex is enthalpy driven, especially at low [salt] (e.g., Delta H(o)(obs)=-20.2 kcal x mol(-","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Mar","modification":"2026-04-29T13:07:05.909Z","creation":"2026-04-07T15:14:17.981Z"},"accession":"S-EPMC2336898","cross_references":{"pubmed":["18237740"],"doi":["10.1016/j.jmb.2007.11.104"]}}