Tandem homologous domains in proteins are susceptible to misfolding through the formation of domain swaps, non-native conformations involving the exchange of equivalent structural elements between adjacent domains. Cutting-edge biophysical experiments have recently allowed the observation of tandem domain swapping events at the single molecule level. In addition, computer simulations have shed light into the molecular mechanisms of domain swap formation and serve as the basis for methods to systematically predict them. At present, the number of studies on tandem domain swaps is still small and limited to a few domain folds, but they offer important insights into the folding and evolution of multidomain proteins with applications in the field of protein design.

中文翻译：

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串联域交换：多域蛋白错误折叠的决定因素。

蛋白质中的串联同源结构域易于通过结构域交换（涉及相邻结构域之间等效结构元件的交换）的非天然构象形成而错误折叠。尖端的生物物理实验最近允许在单分子水平上观察串联结构域交换事件。此外，计算机模拟揭示了域交换形成的分子机制，并为系统地预测它们的方法奠定了基础。目前，关于串联结构域互换的研究数量仍然很少，并且仅限于几个结构域折叠，但是它们为多结构域蛋白的折叠和进化及其在蛋白质设计领域的应用提供了重要的见识。