Mechanics and energetics of protein coordination (or how proteins row)

Molecular motors are protein assemblies that convert chemical energy into mechanical motion through coordinated conformational changes. Efficient activity requires precise temporal and spatial coordination across parts of these assemblies. It remains unclear how such collective behaviour emerges in hexameric motors. In the first part of this talk, I will present a theoretical framework for the collective dynamics of hexameric ATPases, modelled as coupled phase oscillators. Multiple modes of operation observed experimentally emerge naturally from the proposed model. I further show how the model can be applied to interpret previously published data from biochemical assays on motors with mutant subunits. In the second part, I will focus on the AAA+ motor RuvB as a structural case study. Using an elasticity-based energy metric, I will show how to bridge structural data obtained from experimental approaches such as cryo-EM to the kinetic toy model introduced earlier. This work highlights how the energetics of coordination shape mechanochemical cycles, linking single-molecule physics and structural biology.