标题： 生物分子紧束缚模型的电荷转移数据库，来源于数千种蛋白质 显示英文标题

标题： Charge Transfer Database for Bio-molecule Tight Binding Model Derived from Thousands of Proteins

摘要： 电荷转移反应在真实蛋白质中的各向异性特征不能被忽视，这是由于生物分子的高度复杂的化学结构。 在本工作中，我们通过计算所有20*20可能的氨基酸侧链组合中的电荷转移耦合，首次对蛋白质复合物中的电荷转移偏好进行了大规模定量评估，这些组合来自于数千个蛋白质复合物的高质量结构中提取的。 电荷转移数据库定量地显示了数百万种氨基酸侧链组合之间的电荷转移耦合的显著特征。 电荷转移耦合的知识图谱表明，仅有一个平均或代表性结构不能被视为真实蛋白质中典型的电荷转移偏好。 这个数据驱动的模型为我们提供了一种替代方法，基于结构相似性全面理解成对的电荷转移耦合参数，而无需任何关于化学相互作用的化学直觉知识。 显示英文摘要

摘要： The anisotropic feature of charge transfer reactions in realistic proteins cannot be ignored, due to the highly complex chemical structure of bio-molecules. In this work, we have performed the first large-scale quantitative assessment of charge transfer preference in protein complexes by calculating the charge transfer couplings in all 20*20 possible amino acid side chain combinations, which are extracted from available high-quality structures of thousands of protein complexes. The charge transfer database quantitatively shows distinct features of charge transfer couplings among millions of amino acid side-chains combinations. The knowledge graph of charge transfer couplings reveals that only one average or representative structure cannot be regarded as the typical charge transfer preference in realistic proteins. This data driven model provides us an alternative route to comprehensively understand the pairwise charge transfer coupling parameters based structural similarity, without any require of the knowledge of chemical intuition about the chemical interactions.