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... 0.1 μM with an n value of 1.00 ± 0.1 indicating one binding site per hHint1 monomer. Bio-AMS binds approximately 11 and 209 fold more tightly than TrpGc and GMP. The thermodynamic parameters are listed in Table.1. The binding of Bio-AMS is solely enthalpically driven with an unfavorable entropic component. The increased enthalpic contribution indicates that interaction between protein and ligand is primarily driven by hydrogen bonding and electrostatic interactions, while unfavorable entropy indicates minimal contribution from the potential hydrophobic interaction of the biotin side chain with the protein. In addition the thermodynamic parameters indicated that the binding affinity differences observed with Bio-AMS and TrpGc can be primarily attributed to the increased enthalpic contribution resulting in the overall increase in the favorable free energy of binding.
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