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Self-Assembly of a Designed Nucleoprotein Architecturethrough Multimodal Interactions

机译:设计的蛋白结构的自组装通过多式联运

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摘要

The co-self-assembly of proteins and nucleic acids (NAs) produces complex biomolecular machines (e.g., ribosomes and telomerases) that represent some of the most daunting targets for biomolecular design. Despite significant advances in protein and DNA or RNA nanotechnology, the construction of artificial nucleoprotein complexes has largely been limited to cases that rely on the NA-mediated spatial organization of protein units, rather than a cooperative interplay between protein- and NA-mediated interactions that typify natural nucleoprotein assemblies. We report here a structurally well-defined synthetic nucleoprotein assembly that forms through the synergy of three types of intermolecular interactions: Watson–Crick base pairing, NA–protein interactions, and protein–metal coordination. The fine thermodynamic balance between these interactions enables the formation of a crystalline architecture under highly specific conditions.
机译:蛋白质和核酸(NA)的共同自我组装产生了复杂的生物分子机器(例如,核糖体和端粒酶),代表了生物分子设计中一些最艰巨的目标。尽管蛋白质和DNA或RNA纳米技术取得了重大进展,但人工核蛋白复合物的构建在很大程度上限于依赖NA介导的蛋白质单元空间组织的情况,而不是依赖于蛋白质和NA介导的相互作用之间的协同相互作用的情况。代表天然核蛋白装配体。我们在这里报告结构清晰的合成核蛋白组装体,它是通过三种分子间相互作用的协同作用形成的:沃森-克里克碱基配对,NA-蛋白质相互作用和蛋白质-金属配位。这些相互作用之间的良好的热力学平衡使得能够在高度特定的条件下形成晶体结构。

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