Through optimization of the linker region and key stabilizing mutations, it has been possible to improve the stability of the circularly permuted (cp) Trp‐cage miniprotein. However, even the most stable Trp‐cage circular permutants are still less stable than the analogous standard topology (std) Trp‐cages. Extending mutational studies of Trp‐cage fold stability to cp‐species, including analogs lacking chain terminal charges, has uncovered and quantitated some additional stabilizing and destabilizing interactions. Upon protonation, the circular permutants are destabilized to a much greater extent than the standard topology series. End effects, particularly Coulombic interactions, appear to be more important for the cp‐series while the Y10/P4 interaction in the cp‐series is not as significant a stabilizing feature as the corresponding Y3/P19 in the standard topology series.