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Kinetic Control of One-Pot Trans-Splicing Reactions by Using a Wild-Type and Designed Split Intein

机译:使用野生型和设计的拆分内含子进行一锅反式剪接反应的动力学控制

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摘要

Coulombic forces play an important role in facilitating protein-protein interactions. It has been demonstrated that a strong electrostatic potential between two interacting proteins correlates with a fast rate of association and a strong binding affinity. Indeed, this principle has been exploited to enhance the binding properties of engineered protein interfaces. Nonetheless, little research has focused on utilizing intermolecular ion pairs to modulate specificity in protein-protein interactions. Naturally split inteins are a potentially interesting system for engineering electrostatically driven specificity, as the formation of a catalytically competent structure requires the association of two oppositely charged protomers.
机译:库仑力在促进蛋白质-蛋白质相互作用中起重要作用。已经证明,两个相互作用蛋白之间的强静电势与快速缔合速率和强结合亲和力相关。实际上,已经利用该原理来增强工程蛋白界面的结合特性。然而,很少有研究集中在利用分子间离子对来调节蛋白质-蛋白质相互作用中的特异性。天然分裂的内含蛋白是一种工程化静电驱动特异性的潜在有趣系统,因为形成催化活性结构需要结合两个带相反电荷的protomer。

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