Efimov A V, Boshkova E A
Bioorg Khim. 2014 Nov-Dec;40(6):665-72. doi: 10.1134/s1068162014060077.
In the present study, two possible mechanisms of protein folding are analized. One of them is based on the hypothesis that at the first step of protein folding a nucleus is formed and then the remaining part of the molecule or domain is folded around it. For example, β-proteins containing 3β-corners can fold in this way. According to the other mechanism, the three-dimensional structure of proteins is formed as a result of interactions between "ready-made" building blocks. Analysis of structural features of the 3β-corners and features of their amino asid sequences enable us to conclude that the 3β-corner can fold into its unique structure per se and can act as a nucleus or "ready-made" building block in protein folding. The larger protein structures can be obtained by stepwise addition of β-strands to the 3β-corner in accordance with a restricted set of rules as shown in the corresponding structural tree, which is available at http://strees.protres.ru/. On the other hand, complementary interactions of the two 3β-corners can result in formation of the fold that is observed in the serine protease domain and similar proteins.
在本研究中，分析了蛋白质折叠的两种可能机制。其中一种基于这样的假设：在蛋白质折叠的第一步形成一个核，然后分子或结构域的其余部分围绕它折叠。例如，含有3个β转角的β蛋白可以以这种方式折叠。根据另一种机制，蛋白质的三维结构是“现成”构建块之间相互作用的结果。对3个β转角的结构特征及其氨基酸序列特征的分析使我们能够得出结论，3个β转角本身可以折叠成其独特的结构，并且可以在蛋白质折叠中充当核或“现成”构建块。按照如相应结构树（可在http://strees.protres.ru/获取）中所示的一组受限规则，通过将β链逐步添加到3个β转角上，可以获得更大的蛋白质结构。另一方面，两个3个β转角的互补相互作用可导致在丝氨酸蛋白酶结构域和类似蛋白质中观察到的折叠的形成。
