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Lookup NU author(s): Professor Steve Homans
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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 ΔG°int at 308 K for the 1-, 2-, 3-, and 6-hydroxyl groups of galactose is remarkably constant (−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 (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.
Author(s): Daranas AH, Shimizu H, Homans SW
Publication type: Article
Publication status: Published
Journal: Journal of the American Chemical Society
ISSN (print): 0002-7863
ISSN (electronic): 1943-2984
Publisher: American Chemical Society
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