Skewness and Kurtosis in Statistical Kinetics
arXiv:1510.03279 · doi:10.1103/PhysRevLett.115.188103
Abstract
We obtain lower and upper bounds on the skewness and kurtosis associated with the cycle completion time of unicyclic enzymatic reaction schemes. Analogous to a well known lower bound on the randomness parameter, the lower bounds on skewness and kurtosis are related to the number of intermediate states in the underlying chemical reaction network. Our results demonstrate that evaluating these higher order moments with single molecule data can lead to information about the enzymatic scheme that is not contained in the randomness parameter.
5+3 pages, 4 figures
References in corpus (2)
Cited by in corpus (14)
- Optimal stochastic restart renders fluctuations in first passage times universal
- Universal bounds on current fluctuations
- Universal bound on the efficiency of molecular motors
- Single-molecule theory of enzymatic inhibition predicts the emergence of inhibitor-activator duality
- Phase transition in thermodynamically consistent biochemical oscillators
- Thermodynamic uncertainty relation for first-passage times on Markov chains
- First-passage times in renewal and nonrenewal systems
- Quantifying fluctuations in reversible enzymatic cycles and clocks
- Skewness and Kurtosis in Stochastic Thermodynamics
- Brownian particle in a Poisson-shot-noise active bath: exact statistics, effective temperature, and inference
- Critical heat current fluctuations in Curie-Weiss model in and out of equilibrium
- Nonequilibrium fluctuation-response relations for state-current correlations
- Bounds on skewness and kurtosis of steady state currents
- Random walks on modular chains: Detecting structure through statistics