Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5375721 | Chemical Physics | 2008 | 5 Pages |
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
Authors
Andrzej Molski,