Molecular simulations of metal-coupled protein folding
Molecular simulations of metal-coupled protein folding
复制标题
金属耦合蛋白质折叠的分子模拟
DOI：
10.1016/j.sbi.2014.11.006
复制
发表时间：
2015-02-01
影响因子：
6.8
通讯作者：
Wang, Wei
中科院分区：
文献类型：
--
作者：
Li, Wenfei;Wang, Jun;Wang, Wei
许多蛋白质需要金属辅因子的帮助才能正常发挥功能。由于金属结合的参与，这些金属蛋白的折叠可能要复杂得多。近年来，已经开发了几种计算方法来揭示金属偶联蛋白质折叠的基本特征，从量子力学（QM）到原子和粗粒度（CG）模拟。这些理论工具在解决金属结合引起的多尺度困难方面取得了巨大的成功，并为金属蛋白质的折叠机制提供了新的见解。本文首先讨论了金属配位的相互作用特征，然后介绍了几种计算模型及其在金属耦合折叠中的应用。最后，我们讨论了金属结合对蛋白质能量景观的影响，并提出了一些观点。
Many proteins require help from metal cofactors to function properly. Due to the involvement of metal binding, folding of these metalloproteins can be much more complicated. In recent years, several computational methods have been developed to reveal the essential features of metal-coupled protein folding, ranging from quantum mechanics (QM) to atomistic and coarse-grained (CG) simulations. These theoretical tools have achieved great successes in solving the multiscale difficulties arising from metal binding, and provided new insights into the mechanisms of metalloprotein folding. In this review, we first discuss the interaction features of metal-coordination and then introduce several computational models and their applications in metal-coupled folding. Finally we discuss the effects of metal-binding on the protein energy landscape, which is followed by some perspectives.