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摘要翻译：
细胞骨架是以聚合蛋白为基础的自组织网络：肌动蛋白、微管蛋白，并由运动蛋白驱动，如肌球蛋白、动蛋白和动力蛋白。它们积极的达尔文进化使它们能够接近优化的功能（自组织临界性）。我们的理论分析使用水病理波来识别和对比聚合的$α$和$β$微管蛋白单体之间的功能差异，它们在长度和二级结构上相似，并且具有难以区分的系统发育树。我们展示了进化如何改善水驱动的灵活性，特别是对$\α$微管蛋白，从而促进异二聚体微管的组装，与最近的原子模拟和拓扑模型一致。我们得出的结论是，20世纪的技术限制导致了系统发育分析无法识别功能特异性的正达尔文进化。这些问题可以通过基于热力学标度和水病理模平均的21世纪定量数学方法来克服。我们最令人惊讶的结果是发现了大水平集，特别是在疏水极值中，具有热力学上的一阶和二阶尺度水波。我们的计算包括由分形描述的水-蛋白质相互作用。我们还建议了一个急需的纠正大蛋白质药物开发成本。
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英文标题：
《Self-Organized Networks with Long-Range Interactions: Tandem Darwinian
Evolution of $\alpha$ and $\beta$ Tubulin》
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作者：
J. C. Phillips
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最新提交年份：
2020
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分类信息：
一级分类：Quantitative Biology 数量生物学
二级分类：Other Quantitative Biology 其他定量生物学
分类描述：Work in quantitative biology that does not fit into the other q-bio classifications
不适合其他q-bio分类的定量生物学工作
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英文摘要：
Cytoskeletons are self-organized networks based on polymerized proteins: actin, tubulin, and driven by motor proteins, such as myosin, kinesin and dynein. Their positive Darwinian evolution enables them to approach optimized functionality (self-organized criticality). Our theoretical analysis uses hydropathic waves to identify and contrast the functional differences between the polymerizing $\alpha$ and $\beta$ tubulin monomers, which are similar in length and secondary structures, as well as having indistinguishable phylogenetic trees. We show how evolution has improved water-driven flexibility especially for $\alpha$ tubulin, and thus facilitated heterodimer microtubule assembly, in agreement with recent atomistic simulations and topological models. We conclude that the failure of phylogenetic analysis to identify functionally specific positive Darwinian evolution has been caused by 20th century technical limitations. These are overcome using 21st century quantitative mathematical methods based on thermodynamic scaling and hydropathic modular averaging. Our most surprising result is the identification of large level sets, especially in hydrophobic extrema, with both thermodynamically first- and second-order scaled water waves. Our calculations include explicitly long-range water-protein interactions described by fractals. We also suggest a much-needed corrective for large protein drug development costs.
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PDF链接：
https://arxiv.org/pdf/2008.08668
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