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. 2003 Nov;85(5):2845–2853. doi: 10.1016/S0006-3495(03)74707-9

FIGURE 3.

FIGURE 3

Insights into the relative mutant stabilities can be explained by scrutinizing electrostatic potentials. The E3A mutant is stabilized (versus the wild-type) through elimination of the destabilizing E3:E66 charge repulsion. The E3A/A46E mutant is destabilized, largely due to the E46:E66 and E46:CT repulsions. The E3A/A46K mutant is one of the most stable CSP mutants investigated here. The stability gained from the E3A mutation is complemented by favorable K46:E66 and K46:CT ion pairs on the protein surface. Electrostatic potentials are rendered in blue and red at ±3.0 kcal/mol/e, respectively. The above results are quantified using UHBD calculated electrostatic energies (Table 3).