Physics – Biological Physics
Scientific paper
2008-01-09
Phys. Rev. E 78, 010901(R), 2008
Physics
Biological Physics
4 pages, 1 figure v2: Published version, minor corrections in response to referee comments
Scientific paper
10.1103/PhysRevE.78.010901
The first passage times for enzymatic turnovers in non-equilibrium steady state display a statistical symmetry property related to non-equilibrium fluctuation theorems, that makes it possible to extract the chemical driving force from single molecule trajectories in non-equilibrium steady state. Below, we show that this system violates the general expectation that the number of decay constants needed to fit a first passage time distribution reflects the number of states in the escape problem. In fact, the structure of the kinetic mechanism makes half of the decay times vanish identically from the turnover time distribution. The terms that cancel out correspond to the eigenvalues of a certain sub-matrix of the master equation matrix for the first exit time problem. We discuss how these results make modeling and data analysis easier for such systems, and how the turnovers can be measured.
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