Trypsin-like serine proteases are a group of homologous enzymes which exert multiple roles in both vertebrate and invertebrate organisms. Key properties of these enzymes include their activation from an inactive zymogen form to their active form by cleavage of residues in their N-terminus, the presence of a conserved catalytic triad of residues, and the existence of different patterns of substrate selectivity for residue cleavage between the various members of this protein family. In this article, we apply the decomposition of residue coevolution networks computational method to find sets of residues related to some of these key properties, especially to zymogen activation. Positive selection detection, normal modes analysis, and the calculation of thermal couplings between the bovine trypsinogen and bovine trypsin structures residues yielded further information for understanding the zymogen activation process and highlighted the importance of some of the coevolved set residues during these transitions.

中文翻译：

---

共同进化的位置代表了胰蛋白酶样丝氨酸蛋白酶蛋白家族中的关键功能特性。

胰蛋白酶样丝氨酸蛋白酶是一组同源酶，它们在脊椎动物和无脊椎动物中都起着多种作用。这些酶的关键特性包括：通过裂解其N末端的残基将其从无活性的酶原形式激活为活性形式，存在保守的残基催化三联体，以及存在不同的底物选择性裂解底物选择性模式该蛋白质家族的各个成员。在本文中，我们应用残基协同进化网络的分解计算方法来查找与这些关键特性（尤其是酶原激活）相关的残基组。正选择检测，正常模式分析，