Water and protein movements in ligand-receptor interactions.
I have recently developed a novel method `mutual repulsion' for simulating ligand unbindingfrom receptor. Combined with adiabatic switching,this method can evaluate the free energy change of unbinding. Mutualrepulsion has been applied to the bovine serum retinol-bindingprotein-retinol complex (1HBP). Large changes in amino acid configurationis observed in only three residues at the mouth of the binding site. Thechange in water structure around the ligand, from bulk-phase tohydrophobic hydration, as retinol unbinds, is also described.
Department of Biochemistry, University of Cambridge, Cambridge, CB2 1QW United Kingdom.
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hydrophobic interaction; ligand-receptor interaction; molecular dynamics; protein movement; retinol; water