In this article, we investigated the structural and dynamical evolutionary behaviour of a set of ten thioredoxin proteins as formed by three extant forms and seven resurrected ones in laboratory. Starting from the crystallographic structures, we performed all-atom molecular dynamics simulations and compare the trajectories in terms of structural and dynamical properties. Interestingly, the structural properties related to the protein density (i.e. the number of residues divided by the excluded molecular volume) well describe the protein evolutionary behaviour. Our results also suggest that the changes in sequence as occurred during the evolution have affected the protein essential motions, allowing us to discriminate between ancient and extant proteins in terms of their dynamical behaviour. Such results are yet more evident when the bacterial, archaeal and eukaryotic thioredoxins are separately analysed.

中文翻译：

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蛋白质可观察空间中的进化模式：硫氧还蛋白的情况。

在本文中，我们研究了在实验室中由三种现存形式和七种复活形式形成的十种硫氧还蛋白蛋白的结构和动力学进化行为。从晶体结构开始，我们进行了全原子分子动力学模拟，并比较了结构和动力学性质的轨迹。有趣的是，与蛋白质密度有关的结构特性（即残基数除以排除的分子体积）很好地描述了蛋白质的进化行为。我们的研究结果还表明，进化过程中发生的序列变化影响了蛋白质的基本运动，从而使我们能够根据其动态行为来区分古代蛋白质和现存蛋白质。当细菌，