论文标题
Alphafold预测最复杂的蛋白结和复合蛋白结
AlphaFold predicts the most complex protein knot and composite protein knots
论文作者
论文摘要
计算机人工智能系统Alphafold最近预测了以前未知的三维蛋白质结构。为了以较高的自信评分为子集，我们对蛋白质主链表现出罕见拓扑复杂性（即打结）的情况分析了这些预测。除其他外，我们还发现了一个$ 7_1 $的结，这是蛋白质中有史以来最复杂的结，以及几个由两个甲基转移酶或碳纤维性赤铁酶结构域组成的6个跨性复合结，每个结构都包含一个简单的Trefoil结。这些深层嵌入的复合结显然是通过基因复制和打结二聚体的互连而发生的。最后，我们报告了两个新的五加跨结，包括第一个$ 5_1 $ - 结。我们的分析结构列表构成了未来实验研究的基础，以确认这些新型打结的拓扑结构并探索其复杂的折叠机制。
The computer artificial intelligence system AlphaFold has recently predicted previously unknown three-dimensional structures of thousands of proteins. Focusing on the subset with high-confidence scores, we algorithmically analyze these predictions for cases where the protein backbone exhibits rare topological complexity, i.e. knotting. Amongst others, we discovered a $7_1$-knot, the most topologically complex knot ever found in a protein, as well several 6-crossing composite knots comprised of two methyltransferase or carbonic anhydrase domains, each containing a simple trefoil knot. These deeply embedded composite knots occur evidently by gene duplication and interconnection of knotted dimers. Finally, we report two new five-crossing knots including the first $5_1$-knot. Our list of analyzed structures forms the basis for future experimental studies to confirm these novel knotted topologies and to explore their complex folding mechanisms.
