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Stability of ligand-induced protein conformation influences affinity in maltose-binding protein
Journal of Molecular Biology
Our understanding of what determines ligand affinity of proteins is poor, even with high-resolution structures available. Both the non-covalent ligand-protein interactions and the relative free energies of available conformations contribute to the affinity of a protein for a ligand. Distant, non-binding site residues can influence the ligand affinity by altering the free energy difference between a ligand-free and ligand-bound conformation. Our hypothesis is that when different ligands inducedoi:10.1016/j.jmb.2021.167036 pmid:33957147 fatcat:52kn3g6y5vdatb54dt63lpjcpy