Abstract
Protein machines carry out specific tasks in the cell by alternating chemical steps with conformational transitions. Single-molecule FRET spectroscopy is a powerful tool for exposing large-scale function-related motions. We recently developed a novel maximum likelihood algorithm for the analysis of single-molecule experiments, which can track conformational dynamics even on the microsecond time scale (Pirchi et al., JPC B 2016, 120, 13065). We used this algorithm to study two protein machines, the abundant enzyme adenylate kinase (AK) and the disaggregation machine ClpB, finding in both cases surprisingly fast motions.
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