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Evaluates metal ion-induced dimer formation in proteins, suggesting new design strategies.
and the histidine residues within the His-Pro repeats. This predicted structure remained stable during 100-ns molecular dynamics simulations. These experimental and computational evaluations suggest that the insertion of His-Pro repeats into loops is an effective strategy for designing metal ion-induced dimers suggestive of 3D domain-swapped dimers. Our results provide insights into expanding the design space of artificial metal ion-dependent protein dimers and advancing our understanding of the structural principles of metalloproteins.
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Shiga et al. (2026) studied this question.
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