Novel electrostatic mechanism for mode of action by N-acetylated proteins: cell signaling and phosphorylation.
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.
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