Atomic force microscopy is a powerful tool capable of resolving the structure of molecules under near-physiological conditions. Samples can be imaged in their native state: fully hydrated and at biologically relevant temperatures. No additional sample processing, such as fixation, coating, and dehydration, is required. A key strength of the AFM is its ability to monitor dynamic events. Due to its minimal sample preparation, the interaction between molecules and the response of molecules to external factors can be observed. Another capability is the AFM’s ability to measure the mechanical properties of molecules. Piconewton forces can be detected and intra- and inter-molecular forces can be measured. This allows researchers to increase their understanding of protein dynamics, such as how proteins are assembled and the forces needed to unravel them.