Article ID Journal Published Year Pages File Type
5375721 Chemical Physics 2008 5 Pages PDF
Abstract
In this work we have simulated a stochastic model of single-molecule enzymatic kinetics and applied several statistics to find whether substrate fluctuations can cause significant deviations from the standard single-molecule Michaelis-Menten kinetics. We have found that substrate fluctuations can be detected under favorable conditions (i.e. for fast irreversible binding) when long turnover time trajectories are analyzed. However, for reversible and/or slow intrinsic binding substrate fluctuations may be difficult to observe experimentally.
Related Topics
Physical Sciences and Engineering Chemistry Physical and Theoretical Chemistry
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