Force-induced Unbinding Dynamics in a Multidimensional Free Energy Landscape

TL;DR

This paper develops a theoretical framework for understanding how force influences the unbinding process of biomolecules on a multidimensional energy landscape, highlighting conditions where a simplified one-dimensional model is valid.

Contribution

It introduces a theoretical analysis of force-induced unbinding on a 2D energy surface, clarifying when a 1D approximation accurately describes rupture rates.

Findings

Effective 1D description is valid for narrow transition states and high activation barriers.

Force-dependent rupture rates can be accurately modeled under specific energetic conditions.

Coupling between internal dynamics and rupture process is crucial for understanding unbinding behavior.

Abstract

We examined theory for force-induced unbinding on a two-dimensional free energy surface where the internal dynamics of biomolecules is coupled with the rupture process under constant tension f. We show that only if the transition state ensemble is narrow and activation barrier is high, the f-dependent rupture rate in the 2D potential surface can faithfully be described using an effective 1D energy profile.