Understanding microsecond dynamics of protein machines with single-molecule fluorescence

Protein machines carry out specific tasks in the cell by alternating chemical steps with conformational/structural transitions. Single-molecule fluorescence spectroscopy is a powerful tool for exposing large-scale function-related motions. We recently developed a sophisticated maximum likelihood algorithm for the analysis of single-molecule experiments, which can track conformational dynamics even on the microsecond time scale. In the lecture, I will show how this novel analysis helped us understanding the dynamics of two machines, an abundant enzyme and a protein that rescues other proteins from aggregation.