Manipulating single enzymes by an external harmonic force

dc.creatorLomholt, Michael A.
dc.creatorUrbakh, Michael
dc.creatorMetzler, Ralf
dc.creatorKlafter, Joseph
dc.date2006-11-03
dc.date2007-04-16
dc.date.accessioned2026-07-07T07:57:14Z
dc.date.available2026-07-07T07:57:14Z
dc.descriptionWe 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.
dc.description4 pages, 6 figures, minor changes, to appear in Phys. Rev. Lett
dc.identifierhttps://arxiv.org/abs/q-bio/0611011
dc.identifierhttp://arxiv.org/abs/q-bio/0611011
dc.identifierPhys. Rev. Lett. 98, 168302 (2007)
dc.identifierdoi:10.1103/PhysRevLett.98.168302
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/127577
dc.subjectBiomolecules
dc.subjectStatistical Mechanics
dc.titleManipulating single enzymes by an external harmonic force
dc.typetext

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