Stochastic simulation of enzyme-catalyzed reactions with disparate timescales.

ABSTRACT: Many physiological characteristics of living cells are regulated by protein interaction networks. Because the total numbers of these protein species can be small, molecular noise can have significant effects on the dynamical properties of a regulatory network. Computing these stochastic effects is made difficult by the large timescale separations typical of protein interactions (e.g., complex formation may occur in fractions of a second, whereas catalytic conversions may take minutes). Exact stochastic simulation may be very inefficient under these circumstances, and methods for speeding up the simulation without sacrificing accuracy have been widely studied. We show that the "total quasi-steady-state approximation" for enzyme-catalyzed reactions provides a useful framework for efficient a

SUBMITTER: Barik D 

PROVIDER: S-EPMC2553150 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature