作者: Gregory K. Schenter , H. Peter Lu , X. Sunney Xie
DOI: 10.1021/JP992324J
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摘要: Real-time observation of enzymatic turnovers single molecules has revealed non-Markovian dynamical behavior. Although chemical kinetics (such as the Michaelis-Menten mechanism) are sufficient to describe average behavior an ensemble molecules, statistical analysis single-molecule fluorescence time trace reveals fluctuations in rate activation step. These attributed slow protein conformations. In this paper, we discuss models disorder and relate them observables molecule experiments. Simulations based on a discrete multistate model diffusive compared with experiment data. The role various correlation functions, including higher order interpretation underlying dynamics is discussed.