Aaron L. Lucius

This study reveals that Hsp104, an AAA+ ATPase, functions as a bidirectional, processive translocase by switching direction through biased stochastic conformational transitions.

This paper measures the ATP-dependent unfolding and translocation rates of folded substrates by ClpA and ClpAP, showing differential coupling to ATP binding and allosteric regulation by ClpP.

This paper quantifies how E. coli ClpB unfolds and translocates protein substrates, showing ATP-dependent changes in step-size and processivity.

This study uses a single turnover stopped-flow fluorescence method to show ClpB catalyzes processive protein unfolding at ~0.9 aa/s with a step-size of ~60 amino acids.