Single‐molecule tethered particle motion to study protein‐DNA interaction

Single-molecule techniques have been demonstrated as powerful tools to investigate individual protein-DNA interactions that are difficult to access by conventional biochemical techniques. These methods are popularly used to obtain valuable and detailed molecular mechanisms of enzyme functions. Currently, we have used single-molecule tethered particle motion to investigate protein-DNA interactions, including homologous recombination, site-specific recombination, DNA package, and the nucleosome remodeling process, and useful information was obtained. Here, we will describe the experimental designs and present the information obtained.