Single-molecule characterization of the iLID system in live bacterial cells

Abstract

The development of single-molecule tracking (SMT) microscopy has enabled high resolution, live-cell imaging of protein motion in real time. The diffusion rate of the tracked protein can be used to deduce protein-protein interactions at specific subcellular locations, because diffusion is dependent on the size of the protein complex. However, the assignment and validation of diffusive states to specific oligomeric species relies on statistical parameter estimation and, in many cases, deletion or mutation of binding partners that disrupt the protein-protein interaction in question.