Calculating the force-dependent unbinding rate of biological macromolecular bonds from force-ramp optical trapping assays.

ABSTRACT: The non-covalent biological bonds that constitute protein-protein or protein-ligand interactions play crucial roles in many cellular functions, including mitosis, motility, and cell-cell adhesion. The effect of external force ([Formula: see text]) on the unbinding rate ([Formula: see text]) of macromolecular interactions is a crucial parameter to understanding the mechanisms behind these functions. Optical tweezer-based single-molecule force spectroscopy is frequently used to obtain quantitative force-dependent dissociation data on slip, catch, and ideal bonds. However, analyses of this data using dissociation time or dissociation force histograms often quantitatively compare bonds without fully characterizing their underlying biophysical properties. Additionally, the results of histogram-

SUBMITTER: Paul A 

PROVIDER: S-EPMC8741823 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature