FEATHER: Automated Analysis of Force Spectroscopy Unbinding and Unfolding Data via a Bayesian Algorithm.

ABSTRACT: Single-molecule force spectroscopy (SMFS) provides a powerful tool to explore the dynamics and energetics of individual proteins, protein-ligand interactions, and nucleic acid structures. In the canonical assay, a force probe is retracted at constant velocity to induce a mechanical unfolding/unbinding event. Next, two energy landscape parameters, the zero-force dissociation rate constant (k_o) and the distance to the transition state (Δx^‡), are deduced by analyzing the most probable rupture force as a function of the loading rate, the rate of change in force. Analyzing the shape of the rupture force distribution reveals additional biophysical information, such as the height of the energy barrier (ΔG^‡). Accurately quantifying such distributions requires high-

SUBMITTER: Heenan PR 

PROVIDER: S-EPMC6127848 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature