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Understanding hierarchical protein evolution from first principles [Review]

机译:从首要原理了解蛋白质的分层进化[综述]

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摘要

We propose a model that explains the hierarchical organization of proteins in fold families. The model, which is based on the evolutionary selection of proteins by their native state stability, reproduces patterns of amino acids conserved across protein families. Due to its dynamic nature, the model sheds light on the evolutionary time-scales. By studying the relaxation of the correlation function between consecutive mutations at a given position in proteins, we observe separation of the evolutionary time-scales: at short time intervals families of proteins with similar sequences and structures are formed, while at long time intervals the families of structurally similar proteins that have low sequence similarity are formed. We discuss the evolutionary implications of our model. We provide a "profile" solution to our model and find agreement between predicted patterns of conserved amino acids and those actually observed in nature.
机译:我们提出了一个模型,该模型解释了折叠家族中蛋白质的层次结构。该模型基于通过蛋白质的天然状态稳定性对蛋白质进行进化选择,从而重现了跨蛋白质家族保守的氨基酸模式。由于其动态性质,该模型为演化时间尺度提供了启示。通过研究蛋白质给定位置上连续突变之间相关性函数的松弛,我们观察到进化时间尺度的分离:在短时间间隔内形成具有相似序列和结构的蛋白质家族,而在长时间间隔内形成家族形成具有低序列相似性的结构相似的蛋白质。我们讨论了模型的进化含义。我们为模型提供了一个“轮廓”解决方案,并发现了保守氨基酸的预测模式与自然界中实际观察到的模式之间的一致性。

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