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BP: Fachverband Biologische Physik
BP 15: Protein Structure and Single Molecules
BP 15.3: Talk
Wednesday, September 7, 2022, 10:30–10:45, H13
Rebinding kinetics from single-molecule force spectroscopy experiments close to equilibrium — •Jakob Tómas Bullerjahn1 and Gerhard Hummer1,2 — 1Department of Theoretical Biophysics, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany — 2Institute of Biophysics, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany
Analysis of bond rupture data from single-molecule force spectroscopy experiments commonly relies on the strong assumption that the bond dissociation process is irreversible. However, with increased spatiotemporal resolution of instruments it is now possible to observe multiple unbinding-rebinding events in a single pulling experiment. Here, we augment the theory of force-induced unbinding by explicitly taking into account rebinding kinetics, and provide approximate analytic solutions of the resulting rate equations. Furthermore, we use a short-time expansion of the exact kinetics to construct numerically efficient maximum likelihood estimators for the parameters of the force-dependent unbinding and rebinding rates, which pair well with and complement established methods, such as the analysis of rate maps. We provide an open-source implementation of the theory, evaluated for Bell-like rates, which we apply to synthetic data generated by a Gillespie stochastic simulation algorithm for time-dependent rates.