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首页> 外文期刊>Journal of receptor and signal transduction research >Novel electrostatic mechanism for mode of action by N-acetylated proteins: Cell signaling and phosphorylation
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Novel electrostatic mechanism for mode of action by N-acetylated proteins: Cell signaling and phosphorylation

机译:N-乙酰化蛋白质作用方式的新型静电机制:细胞信号传导和磷酸化

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摘要

Although extensive literature exists for N-acetylated proteins, scant knowledge is available concerning resultant mode of action. This review presents a novel mechanism based on electrostatics and cell signaling. There is substantial increase in the amide dipole and electrostatic field (EF) in contrast with the primary amino of the lysine precursor. The EF might serve as a bridge in electron transfer and cell signaling or energetics may play a role. The relationship between N-acetylation and phosphorylation is addressed. EFs may be important in the case of phosphates. Involvement of cell signaling is addressed including mechanistic aspects. As is the case for many aspects of bioaction, an integrated approach involving electrochemistry and cell signaling seems reasonable.
机译:尽管存在大量有关N-乙酰化蛋白质的文献,但关于作用方式的知识很少。这篇综述提出了一种基于静电和细胞信号传导的新型机制。与赖氨酸前体的伯氨基相比,酰胺偶极子和静电场(EF)显着增加。 EF可能充当电子转移的桥梁,细胞信号传导或高能可能发挥作用。解决了N-乙酰化和磷酸化之间的关系。对于磷酸盐,EFs可能很重要。解决了细胞信号传导的参与,包括机械方面。就像生物作用的许多方面一样,涉及电化学和细胞信号转导的整合方法似乎是合理的。

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