dorsal/arxiv
View SchemaDynamical hysteresis in multisite protein modification
| Authors | Edoardo Milotti, Alessio Del Fabbro, Chiara Dalla Pellegrina, Roberto Chignola |
|---|---|
| Categories | |
| ArXiv ID | physics/0702094 |
| URL | https://arxiv.org/abs/physics/0702094 |
Abstract
Multisite protein modification is a ubiquitous mechanism utilized by cells to control protein functions. We have recently proposed a dynamical description of multisite protein modification which embodies all the essential features of the process (E. Milotti, A. Del Fabbro, C. Dalla Pellegrina, and R. Chignola, Physica A, in press), and we have used this model to analyze the stability and the time-scales of this mechanism. The same model can be used to understand how the system responds to stimuli: here we show that it displays frequency-dependent dynamical hysteresis. This behavior closely parallels -- with the due differences -- what is observed in magnetic systems. By selecting model parameters that span the known biological ranges, we find that the frequency-dependent features cover the band of the observed oscillations of molecular intracellular signals, and this suggests that this mechanism may have an important role in cellular information processing.
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"abstract": "Multisite protein modification is a ubiquitous mechanism utilized by cells to\ncontrol protein functions. We have recently proposed a dynamical description of\nmultisite protein modification which embodies all the essential features of the\nprocess (E. Milotti, A. Del Fabbro, C. Dalla Pellegrina, and R. Chignola,\nPhysica A, in press), and we have used this model to analyze the stability and\nthe time-scales of this mechanism. The same model can be used to understand how\nthe system responds to stimuli: here we show that it displays\nfrequency-dependent dynamical hysteresis. This behavior closely parallels --\nwith the due differences -- what is observed in magnetic systems. By selecting\nmodel parameters that span the known biological ranges, we find that the\nfrequency-dependent features cover the band of the observed oscillations of\nmolecular intracellular signals, and this suggests that this mechanism may have\nan important role in cellular information processing.",
"arxiv_id": "physics/0702094",
"authors": [
"Edoardo Milotti",
"Alessio Del Fabbro",
"Chiara Dalla Pellegrina",
"Roberto Chignola"
],
"categories": [
"physics.bio-ph",
"q-bio.MN"
],
"title": "Dynamical hysteresis in multisite protein modification",
"url": "https://arxiv.org/abs/physics/0702094"
},
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