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Force spectroscopy of a single artificial biomolecule bond: The Kramers’ high-barrier limit holds close to the critical force
Author(s) -
Julien Husson,
Marileen Dogterom,
Frédéric Pincet
Publication year - 2009
Publication title -
the journal of chemical physics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.071
H-Index - 357
eISSN - 1089-7690
pISSN - 0021-9606
DOI - 10.1063/1.3077010
Subject(s) - force spectroscopy , biomolecule , optical tweezers , physics , molecular physics , chemistry , chemical physics , statistical physics , nanotechnology , materials science , molecule , optics , quantum mechanics
We use a minimal system with a single micron-size bead trapped with optical tweezers to investigate the kinetics of escape under force. Surprisingly, the exponential decay of the off rate with the barrier energy is still valid close to the critical force. Hence, the high viscosity approximation derived by Kramers in the case of a high energy barrier holds even for an energy barrier close to the thermal energy. Several recent models describe a single biomolecule bond by a smooth single-barrier energy profile. When this approach is accurate enough, our result justifies the use of Kramers' approximation in the high-force regime, close to the critical force of the system, as done in recent single biomolecule bond studies.

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