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• W1982803402 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 °C. Both the binding constant Kobs and enthalpy ΔH°obs depend strongly on [salt] and anion identity. Formation of the wrapped complex is enthalpy driven, especially at low [salt] (e.g., ΔHoobs = − 20.2 kcal·mol− 1 in 0.04 M KCl). ΔH°obs increases linearly with [salt] with a slope (dΔH°obs/d[salt]), which is much larger in KCl (38 ± 3 kcal·mol− 1 M− 1) than in KF or KGlu (11 ± 2 kcal·mol− 1 M− 1). At 0.33 M [salt], Kobs is approximately 30-fold larger in KGlu or KF than in KCl, and the [salt] derivative SKobs = dlnKobs/dln[salt] is almost twice as large in magnitude in KCl (− 8.8 ± 0.7) as in KF or KGlu (− 4.7 ± 0.6). A novel analysis of the large effects of anion identity on Kobs, SKobs and on ΔH°obs dissects coulombic, Hofmeister, and osmotic contributions to these quantities. This analysis attributes anion-specific differences in Kobs, SKobs, and ΔH°obs to (i) displacement of a large number of water molecules of hydration [estimated to be 1.0(± 0.2) × 103] from the 5340 Å2 of IHF and H′ DNA surface buried in complex formation, and (ii) significant local exclusion of F− and Glu− from this hydration water, relative to the situation with Cl−, which we propose is randomly distributed. To quantify net water release from anionic surface (22% of the surface buried in complexation, mostly from DNA phosphates), we determined the stabilizing effect of GB on Kobs: dlnKobs/d[GB] = 2.7 ± 0.4 at constant KCl activity, indicating the net release of ca. 150 H2O molecules from anionic surface." @default.
• W1982803402 created "2016-06-24" @default.
• W1982803402 creator A5007035329 @default.
• W1982803402 creator A5065525960 @default.
• W1982803402 creator A5070425962 @default.
• W1982803402 date "2008-03-01" @default.
• W1982803402 modified "2023-10-12" @default.
• W1982803402 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" @default.
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• W1982803402 doi "https://doi.org/10.1016/j.jmb.2007.11.104" @default.
• W1982803402 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2336898" @default.
• W1982803402 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18237740" @default.
• W1982803402 hasPublicationYear "2008" @default.
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