Dynamic imaging of single DNA–protein interactions using atomic force microscopy Review Article

Atomic force microscopy (AFM) imaging of static DNA–protein complexes, in air and in liquid, can be used to directly obtain quantitative and qualitative information on the structure of different complexes. For example, DNA length, the location of preferential binding sites for proteins and bending of DNA as a result of the complexation can all be measured. Recording consecutive AFM images of DNA and protein molecules under conditions that they are still able to move and interact, or dynamic AFM imaging, however, can reveal information on the dynamic aspects of the interactions between these molecules. Here, an overview is given of the technical challenges that need to be considered for successful dynamic AFM imaging studies of individual DNA–protein interactions. Necessary technical improvements to the AFM set-up and the development of new sample preparation methods are described in this paper.