In vitro structural analysis reveals that shortening omega-loop D alters human cytochrome c dimer stability, highlighting the critical role of globular protein-protein interactions.
Three-dimensional domain swapping (3D-DS) properties of wild-type human cyt c and its variants, in which one to five residues were deleted from Ω-loop D, were investigated. The cyt c dimer stability generally decreased as more amino acids were deleted from Ω-loop D. However, the del82-85 dimer exhibited a relatively small dissociation rate constant and hydrodynamic size, indicating that protein–protein interactions between the functional globular units play a crucial role in determining the stability of the 3D-DS dimer.
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Ota et al. (2026) studied this question.
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