How the protonation state of a phosphorylated amino acid governs molecular recognition: insights from classical molecular dynamics simulations
How the protonation state of a phosphorylated amino acid governs molecular recognition: insights from classical molecular dynamics simulations
复制标题
磷酸化氨基酸的质子化状态如何控制分子识别：经典分子动力学模拟的见解
DOI：
10.1002/1873-3468.13674
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发表时间：
2019
期刊：
影响因子：
3.5
通讯作者：
Tsumoto Kouhei
中科院分区：
文献类型：
--
作者：
Kawade Raiji;Kuroda Daisuke;Tsumoto Kouhei
蛋白质的理化性质主要由翻译后修饰如氨基酸磷酸化控制。尽管分子动力学模拟已被证明是研究磷酸化对蛋白质结构和动力学影响的有价值的工具，但以前的大多数研究都假设磷酸基团处于未质子化（）状态，尽管质子化状态实际上可能在生理pH下发生变化。在这项研究中，我们对四种不同的蛋白质磷酸化肽复合物在和PO3H−状态下进行了分子动力学模拟。我们的模拟描绘了两种状态之间不同的动力学和能量学，表明磷酸化氨基酸的质子化状态在分子识别中的重要性。
Physicochemical properties of proteins are controlled mainly by post‐translational modifications such as amino acid phosphorylation. Although molecular dynamics simulations have been shown to be a valuable tool for studying the effects of phosphorylation on protein structure and dynamics, most of the previous studies assumed that the phosphate group was in the unprotonated () state, even though the protonation state could in fact vary at physiological pH. In this study, we performed molecular dynamics simulations of four different protein‐phosphorylated peptide complexes both in the and PO3H−states. Our simulations delineate different dynamics and energetics between the two states, suggesting importance of the protonation state of a phosphorylated amino acid in molecular recognition.