Statistical Analyses and Theoretical Models of Single-Molecule Enzymatic Dynamics
Real-time observation of enzymatic turnovers of single molecules has revealed non-Markovian dynamical behavior. Although chemical kinetics (such as the Michaelis-Menten mechanism) are sufficient to describe the average behavior of an ensemble of molecules, statistical analysis of the single-molecule fluorescence time trace reveals fluctuations in the rate of the activation step. These fluctuations are attributed to slow fluctuations of protein conformations. In this paper, we discuss models of the dynamical disorder behavior and relate them to observables of single molecule experiments. Simulations based on a discrete multistate model and a diffusive model are compared with experiment data. The role of various correlation functions, including higher order time correlation functions, in the interpretation of the underlying dynamics is discussed.
- Research Organization:
- Pacific Northwest National Laboratory (PNNL), Richland, WA (US)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 1033481
- Report Number(s):
- PNNL-SA-32157; KC0301020
- Journal Information:
- Journal of Physical Chemistry A, Journal Name: Journal of Physical Chemistry A Journal Issue: 49 Vol. 103; ISSN 1089-5639
- Country of Publication:
- United States
- Language:
- English
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