摘要翻译：
这项工作的主要目的是探索蛋白质点突变如何影响其边缘稳定性，从而影响其进化能力。为了这个目的，我们表明，使用四个经典概念，即莱布尼茨和康德(1768)、梅纳德·史密斯(1970)、爱因斯坦和因费尔德（1961）和安芬森（1973）的概念，足以更好地理解蛋白质进化，从而确定能够控制它的因素。初步结果--没有明确考虑上位性效应--表明点突变时蛋白质边缘稳定性的变化提供了必要和充分的信息，通过玻尔兹曼因子来描述酰胺氢交换保护因子的演化。这一发现是至关重要的，因为它说明了点突变对蛋白质边缘稳定性和与自然状态共存的折叠构象组合的影响，以及在变质作用存在时对出现新折叠和功能的倾向的影响。
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英文标题：
《Proteins Evolution Upon Point Mutations》
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作者：
J.A. Vila
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最新提交年份：
2021
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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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一级分类：Physics        物理学
二级分类：History and Philosophy of Physics        物理学的历史与哲学
分类描述：History and philosophy of all branches of physics, astrophysics, and cosmology, including appreciations of physicists.
物理学、天体物理学和宇宙学的所有分支的历史和哲学，包括物理学家的赏析。
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英文摘要：
  The primary aim of this work is to explore how proteins point mutations impact their marginal stability and, hence, their evolvability. With this purpose, we show that the use of four classic notions, namely, those from Leibniz & Kant (1768), Maynard Smith (1970), Einstein & Infeld (1961), and Anfinsen (1973), is sufficient for a better understanding of the protein-evolution and, consequently, to determine the factors that could control it. The preliminary results -- without considering epistasis effects explicitly -- indicate that the protein marginal-stability change upon point mutations provides the necessary and sufficient information to describe, through a Boltzmann factor, the evolution of the amide hydrogen-exchange protection factors. This finding is of paramount importance because it illustrates the impact of point mutations on both the protein marginal-stability and the ensemble of folded conformations coexisting with the native state and, in the presence of metamorphism, on the propensity for the appearance of new folds and functions.
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PDF链接：
https://arxiv.org/pdf/2111.04199