Abstract
Since its invention in 1986, the atomic force microscope (AFM) has emerged as a flexible and powerful tool for exploring a variety of biological processes, including cell adhesion, protein folding, and protein–protein interactions. This review focuses on the application of the AFM to studies of protein–protein interactions. It describes the commonly used methodologies and reviews the theoretical framework used to analyze single-molecule protein–protein unbinding measurements. Finally, the chapter summarizes recent progress in the field and shows that the AFM provides an excellent tool for probing interactions on the cell surface and for understanding the energy landscapes that govern the dynamics of protein interactions.
