Manipulating single enzymes by an external harmonic force

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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

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Biomolecules, Statistical Mechanics

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http://salesiana.dossiersoluciones.com/handle/123456789/127577

Consulte el texto completo en el siguiente enlace:

https://arxiv.org/abs/q-bio/0611011
 http://arxiv.org/abs/q-bio/0611011
 Phys. Rev. Lett. 98, 168302 (2007)
 doi:10.1103/PhysRevLett.98.168302

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arXiv