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Significance Natural protein sequences have evolved to fold efficiently to their functional forms, traversing a relatively smooth energy surface with minimal frustration. The optimization of stability in de novo-designed proteins, without regard to dynamical processes required for function, can have unintended consequences on energy surfaces. Electrostatic and hydrophobic networks of side chains for Di-III_14, a small βα protein with a natural topology, create a rough energy surface whose high-energy states reflect the progressive unlocking of a tightly packed interior. Unbiased explorations of sequence space can reveal complex properties not seen in natural proteins, expanding our understanding of the relationships among sequence, structure, folding, and function of these ubiquitous biopolymers.

Networks of electrostatic and hydrophobic interactions modulate the complex folding free energy surface of a designed βα protein