Abstract
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.
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