Figure S1 - A Quantitative Measure of Electrostatic Perturbation in Holo and Apo Enzymes Induced by Structural Changes

Invariance of electrostatic perturbation based on radial distance from the active site used to choose interacting residues. In the diphtheria toxin repressor from Corynebacterium diphtheriae, the C-terminal undergoes more electrostatic perturbation compared to the N-terminal, and this change is independent of the radial distance which defines interacting residues (PDF)