Probing structural dynamics and interactions in macromolecular complexes with single-molecule force spectroscopy

Abstract

Many cellular processes involve assemblies of diverse biological molecules acting in concert. Single-molecule force spectroscopy offers a powerful approach for deciphering how the components of such complexes interact dynamically. By applying mechanical forces to individual molecules within the complex, multiple features can be explored, including the conformation of these molecules, the strength of their interactions with other members of the complex, and association/dissociation rates. We discuss recent advances from force spectroscopy studies of complexes involving protein–nucleic acid, protein–protein, and protein-lipid interactions, which provide insight into processes relevant for both biological function and disease.