Thermodynamics of Binding of d-Galactose and Deoxy Derivatives thereof to the l-Arabinose-binding Protein
- 1 September 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 126 (38), 11870-11876
- https://doi.org/10.1021/ja048054m
Abstract
We report the thermodynamics of binding of d-galactose and deoxy derivatives thereof to the arabinose binding protein (ABP). The "intrinsic" (solute-solute) free energy of binding DeltaG degrees (int) at 308 K for the 1-, 2-, 3-, and 6-hydroxyl groups of galactose is remarkably constant (approximately -30 kJ/mol), despite the fact that each hydroxyl group subtends different numbers of hydrogen bonds in the complex. The substantially unfavorable enthalpy of binding (approximately 30 kJ/mol) of 1-deoxygalactose, 2-deoxygalactose, and 3-deoxygalactose in comparison with galactose, cannot be readily accounted for by differences in solvation, suggesting that solute-solute hydrogen bonds are enthalpically significantly more favorable than solute-solvent hydrogen bonds. In contrast, the substantially higher affinity for 2-deoxygalactose in comparison with either 1-deoxygalactose or 3-deoxygalactose derives from differences in the solvation free energies of the free ligands.Keywords
This publication has 22 references indexed in Scilit:
- Thermodynamics of Binding of 2-Methoxy-3-isopropylpyrazine and 2-Methoxy-3-isobutylpyrazine to the Major Urinary ProteinJournal of the American Chemical Society, 2004
- Involvement of Water in Carbohydrate−Protein BindingJournal of the American Chemical Society, 2001
- Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxationJournal of Molecular Biology, 1997
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactionsCell Chemical Biology, 1995
- A Direct Measure of the Contribution of Solvent Reorganization to the Enthalpy of BindingJournal of the American Chemical Society, 1994
- The Entropic Cost of Bound Water in Crystals and BiomoleculesScience, 1994
- NMR order parameters and free energy: an analytical approach and its application to cooperative calcium(2+) binding by calbindin D9kJournal of the American Chemical Society, 1993
- Protein-ligand energetics assessed using deoxy and fluorodeoxy sugars in equilibrium binding and high resolution crystallographic studiesJournal of Molecular Biology, 1992
- Novel stereospecificity of the L-arabinose-binding proteinNature, 1984