bioRxiv · 10.64898/2026.04.02.716112
Synonymous coding significantly affects the domain swapping propensity of myoglobin
Abstract
Co-translational folding is a critical, yet poorly understood, aspect of protein biogenesis due to its transient, heterogeneous, and experimentally inaccessible nature. Using a myoglobin variant engineered towards increased domain swapping, we show that stable dimers formed during heterologous E. Coli expression revert to the monomeric state following denaturation - renaturation and that domain swapping propensity is significantly affected by synonymous coding. Wider implications for the role of synonymous coding in aggregation and disease are discussed.
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Marx, A., Dor, S.. 2026-04-06. Synonymous coding significantly affects the domain swapping propensity of myoglobin. https://doi.org/10.64898/2026.04.02.716112
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