磷酸化氨基酸的质子化状态如何控制分子识别:来自经典分子动力学模拟的见解

IF 3 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Raiji Kawade, Daisuke Kuroda, K. Tsumoto
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引用次数: 7

摘要

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一个有价值的工具,但大多数先前的研究都假设磷酸基团处于未质子化(PO32-)状态,尽管质子化状态实际上可能在生理ph值下发生变化。在本研究中,我们对四种不同的蛋白质-磷酸化肽复合物进行了分子动力学模拟,分别处于PO32-和PO3H -状态。我们的模拟描述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。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
How the protonation state of a phosphorylated amino acid governs molecular recognition: insights from classical molecular dynamics simulations
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 ( PO32- ) 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 PO32- 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.
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来源期刊
FEBS Letters
FEBS Letters 生物-生化与分子生物学
CiteScore
6.60
自引率
2.90%
发文量
303
审稿时长
1 months
期刊介绍: FEBS Letters is one of the world''s leading journals in molecular biology and is renowned both for its quality of content and speed of production. Bringing together the most important developments in the molecular biosciences, FEBS Letters provides an international forum for Minireviews, Research Letters and Hypotheses that merit urgent publication.
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