Manipulating single enzymes by an external harmonic force

Abstract

We study a Michaelis-Menten reaction for a single two-state enzyme molecule, whose transition rates between the two conformations are modulated by an harmonically oscillating external force. In particular, we obtain a range of optimal driving frequencies for changing the conformation of the enzyme thereby controlling the enzymatic activity (i.e. product formation). This analysis demonstrates that it is, in principle, possible to obtain information about particular rates within the kinetic scheme.

4 pages, 6 figures, minor changes, to appear in Phys. Rev. Lett

References in corpus (3)

• Utilizing the information content in two-state trajectories
• Single Molecule Michaelis-Menten Equation beyond Quasi-Static Disorder
• Insight into Resonant Activation in Discrete Systems

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