Intrinsic rates and activation free energies from single-molecule pulling experiments.
By O. Dudko, Gerhard Hummer, Attila Szabó. Physical Review Letters, 2006
735 citations recorded by the source corpus.
We present a unified framework for extracting kinetic information from single-molecule pulling experiments at constant force or constant pulling speed. Our procedure provides estimates of not only (i) the intrinsic rate coefficient and (ii) the location of the transition state but also (iii) the free energy of activation. By analyzing simulated data, we show that the resulting rates of force-induced rupture are significantly more reliable than those obtained by the widely used approach based on Bell's formula. We consider the uniqueness of the extracted kinetic information and suggest guidelines to avoid over-interpretation of experiments.
Subfields: Atomic and Molecular Physics, and Optics, Biophysics
View Paper: https://www.semanticscholar.org/paper/6853a3b0089a2a0e87c3259546929375989e804e
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In Atomic and Molecular Physics, and Optics
In Biophysics
Citations in the corpus
- Discovery Through the Computational Microscope (2009, positive): “…well the force dependency of reaction rates (Schlierf et al., 2004; Garcia-Manyes et al., 2009a, 2009b) and had indeed been refined later (Dudko et al., 2003, 2006, 2008; Best et al., 2008; Guo et al., 2008; Dudko, 2009), it has been used successfully to interpret AFM force versus…”
- Biomolecules under mechanical force (2010, methodology): “(57), has been repeatedly refined using various approximations [135,147,150,313].”
- Theory, analysis, and interpretation of single-molecule force spectroscopy experiments (2008, methodology): “This mapping follows directly from the quasi-adiabatic assumption (22, 26) and is independent of the nature of the underlying free-energy surface.”