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Significance Despite the vast number of known protein topologies, the actual behavior and selective traits of their constituent α- and β-secondary-structure elements remain elusive. The reason is that the high-energy fluctuations associated with their motions in folded proteins are intrinsically difficult to measure. Here, we circumvent this problem by presenting an alternative, and generally applicable, protein-design strategy that activates dynamic swapping of entire α- and β-elements in the folded ground state. We find that the behavior of the α- and β-elements is, indeed, very distinct where the differences in structural and dynamic properties have relevance not only for the understanding of protein function, but also for the mechanism of structural evolution per se.

Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins