Abstract
The load-dependence of reversible product release in myosins is key to understanding how it converts chemical energy into mechanical force. Following the powerstroke and phosphate (Pi) release, the rebinding of Pi to the actomyosin⋅ADP complex is highly load-dependent, but the underlying mechanisms/structures involved remain unclear. Therefore, we introduced a mutation (S217A) into the switch I region of the active site to examine its impact on the load dependence of Pi rebinding to single-headed myosin Va (MV) in a mini-ensemble (∼10 heads) three-bead laser trap assay at 100 uM ATP.
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