Protein functions in cells may be activated or modified by the attachment of several kinds of chemical groups. While protein phosphorylation, i.e., the attachment of a phosphoryl ðPO3 Þ group, is the most studied form of protein modification, and is known to regulate the functions of many proteins, protein behavior can also be modified by nitrosylation, acetylation, methylation, etc. A protein can have multiple modification sites, and displays some form of transition only when enough sites are modified. In a previous paper we have modeled the generic equilibrium properties of multisite protein modification [R. Chignola, C. Dalla Pellegrina, A. Del Fabbro, E. Milotti, Physica A 371 (2006) 463] and we have shown that it can account both for sharp, robust thresholds and for information transfer between processes with widely separated timescales. Here we use the same concepts to expand that analysis starting from a dynamical description of multisite modification: we give analytical results for the basic dynamics and numerical results in an example where the modification chain is cascaded with a Michaelis–Menten step. We modify the dynamics and analyze an example with realistic phosphorylation/dephosphorylation steps, and give numerical evidence of the independence of the allosteric effect from the details of the attachment–detachment processes. We conclude that multisite protein modification is dynamically equivalent to the classic allosteric effect.
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