Department of Physics and Center for Complexity and Biosystems, Università degli Studi di Milano and INFN, via Celoria 16, 20133, Milan, Italy.
Department of Applied Science and Technology, Politecnico di Torino, Corso Duca degli Abruzzi 24, 10129, Turin, Italy.
Eur Biophys J. 2021 Jul;50(5):699-712. doi: 10.1007/s00249-021-01500-0. Epub 2021 Feb 11.
Energetic properties of a protein are a major determinant of its evolutionary fitness. Using a reconstruction algorithm, dating the reconstructed proteins and calculating the interaction network between their amino acids through a coevolutionary approach, we studied how the interactions that stabilise 890 proteins, belonging to five families, evolved for billions of years. In particular, we focused our attention on the network of most strongly attractive contacts and on that of poorly optimised, frustrated contacts. Our results support the idea that the cluster of most attractive interactions extends its size along evolutionary time, but from the data, we cannot conclude that protein stability or that the degree of frustration tends always to decrease.
蛋白质的能量特性是其进化适应性的主要决定因素。我们使用一种重建算法，对重建后的蛋白质进行定年，并通过共进化方法计算它们氨基酸之间的相互作用网络，研究了 890 种属于五个家族的蛋白质的相互作用是如何在数十亿年的时间里进化的。具体来说，我们关注的是最强吸引力的相互作用网络和那些优化不足、受挫的相互作用网络。我们的研究结果支持了这样一种观点，即最具吸引力的相互作用簇在进化过程中会不断扩大其规模，但从数据中，我们无法得出蛋白质稳定性或受挫程度总是降低的结论。
