<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Vander Meulen KA</submitter><funding>NIGMS NIH HHS</funding><pagination>9-27</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2336898</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>377(1)</volume><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(-</pubmed_abstract><journal>Journal of molecular biology</journal><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.</pubmed_title><pmcid>PMC2336898</pmcid><funding_grant_id>R37 GM023467</funding_grant_id><funding_grant_id>GM 23467</funding_grant_id><pubmed_authors>Vander Meulen KA</pubmed_authors><pubmed_authors>Saecker RM</pubmed_authors><pubmed_authors>Record MT</pubmed_authors></additional><is_claimable>false</is_claimable><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.</name><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(-</description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Mar</publication><modification>2026-04-29T13:07:05.909Z</modification><creation>2026-04-07T15:14:17.981Z</creation></dates><accession>S-EPMC2336898</accession><cross_references><pubmed>18237740</pubmed><doi>10.1016/j.jmb.2007.11.104</doi></cross_references></HashMap>