Redox partner interactions are governed by electrostatic complementarity where the electronegative surface of the flavoprotein pairs with the electropositive portion of the P450.
In the above examples, it is clear that the polarization induced by protein protein binding is significant; it enhances the electrostatic complementarity and thus increases the binding energies.
It is clear that the polarization induced upon complexation enhances both electrostatic complementarity and binding.
For selected cases, we have evaluated the physicochemical viability of the predicted interactions in terms of surface complementarity, electrostatic complementarity, and interaction energies at protein interface regions.
For specific cases, we have pursued rigorous evaluation in terms of surface complementarity, electrostatic complementarity, and interaction energy at the interface regions to support the credibility of the predictions made.
Thus, the characteristic surface feature of the native interfaces in Cluster 2 could be the electrostatic complementarity, and it corresponds to the character of f c2.
In order to support this finding, we investigated further in terms of electrostatic complementarity and interfacial residues stabilizing the modeled complex.
Previous studies have concluded that antibody-protein interactions are based on "charge complementarity" and "electrostatic complementarity" [ 58], and that this complementarity is important in defining binding site specificity [ 59].
The three enzymes are structurally essentially identical, and substrate binding occurs in a highly conserved pocket providing shape and electrostatic complementarity to uracil and which is too narrow to accommodate purines.
Collectively, the Cre, Flp and topoisomerase results highlight the contribution of conserved electrostatic complementarity between substrate and active site towards transition state stabilization during site-specific recombination and DNA relaxation.
