Related Experiment Video
Updated: Jun 19, 2026

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
Published on: December 20, 2013
Direct and model free calculation of force-dependent dissociation rates from force spectroscopic data
Leoni Oberbarnscheidt1, Richard Janissen, Filipp Oesterhelt
1Institute of Molecular Physical Chemistry, Heinrich-Heine University, Düsseldorf, Germany.
Abstract:
Force spectroscopy allows testing the free energy landscapes of molecular interactions. Usually, the dependency of the most probable rupture force on the force rate or the shape of the rupture force histogram is fitted with different models that contain approximations and basic assumptions. We present a simple and model free approach to extract the force-dependent dissociation rates directly from the force curve data. Simulations show that the dissociation rates at any force are given directly by the ratio of the number of detected rupture events to the time this force was acting on the bond. To calculate these total times of acting forces, all force curve data points of all curves measured are taken into account, which significantly increases the amount of information which is considered for data analysis compared to other methods. Moreover, by providing force-dependent dissociation rates this method allows direct testing and validating of any energy landscape model.
Related Concept Videos
Force and Potential Energy in One Dimension
IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration
According to Hooke's law, the vibrational frequency is directly proportional to the...
Bond Dissociation Energy and Activation Energy
Acid/Base Strengths and Dissociation Constants
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

