Physics – Biological Physics
Scientific paper
2006-09-26
Physics
Biological Physics
14 figures, major revisions in main text, additional results and extended conclusions
Scientific paper
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 (PO$_3^-$) 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 display 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 {\bf 371}, 463 (2006)) 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.
Chignola Roberto
Fabbro Alessio Del
Milotti Edoardo
Pellegrina Chiara Dalla
No associations
LandOfFree
Dynamics of allosteric action in multisite protein modification does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.
If you have personal experience with Dynamics of allosteric action in multisite protein modification, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Dynamics of allosteric action in multisite protein modification will most certainly appreciate the feedback.
Profile ID: LFWR-SCP-O-261302