Center of Physical Chemistry Test, Shenyang University of Chemical Technology, Shenyang 110142, People's Republic of China.
Phys Chem Chem Phys. 2018 Sep 19;20(36):23301-23310. doi: 10.1039/c8cp01803k.
Theoretical study of the electronic structures of protein is a fundamental challenge in computational biochemistry due to the large size of the systems. The electronic structure of a protein is important for some of the important protein functionalities, such as photosynthesis. In this study, we explored the charge-patching method to calculate the electronic structure of polypeptides. This method generates the charge densities of the systems by patching the charge motifs calculated from small prototype systems. The method was tested on a range of polypeptides, including the glycine polypeptide in 27-ribbon, α-helix, 310-helix, and β-strand structures. After the charge density profiles of these systems were obtained, the electronic structures of these glycine polypeptides were further calculated based on density functional theory (DFT) using a folded-spectrum method. The highest occupied molecular orbital (HOMO) and the lowest unoccupied molecular orbital (LUMO) were analyzed and compared with conventional direct DFT calculations. The charge-patching method results were found to be in good agreement with the directed DFT results.
蛋白质电子结构的理论研究是计算生物化学中的一个基本挑战，因为系统的规模很大。蛋白质的电子结构对于一些重要的蛋白质功能很重要，如光合作用。在这项研究中，我们探索了电荷补丁方法来计算多肽的电子结构。该方法通过从小原型系统计算的电荷模体来生成系统的电荷密度。该方法在一系列多肽上进行了测试，包括 27 条带中的甘氨酸多肽、α-螺旋、310 螺旋和 β-折叠结构。获得这些系统的电荷密度分布后，根据密度泛函理论（DFT）使用折叠光谱法进一步计算这些甘氨酸多肽的电子结构。分析并比较了最高占据分子轨道（HOMO）和最低未占据分子轨道（LUMO）与传统的直接 DFT 计算结果。发现电荷补丁方法的结果与定向 DFT 结果非常吻合。
