Fig. 5
From: Intrinsic enzymatic properties modulate the self-propulsion of micromotors
Conformation of UR and motion behavior of UR-HSMM exposed to AHA. Representative snapshots from MD simulations of a UR in apo state where the flap covering the active site can adopt a closed conformation (purple) and b AHA, which stabilizes wide-open conformations of the flap (teal). The zoom of the active site residues shows catalytic residues in green, nickel atoms in pink, and the AHA inhibitor in yellow. c MD simulated flap distance between Ala440–Ile599 in the apo state (purple) and AHA-bound state (teal). Results are shown as the mean ± standard deviation (s.d.). d Representative 28-s trajectories of UR-HSMM exposed to 500 mM urea and different concentrations of AHA (axis divided into 5 µm fragments). e Average MSD of UR-HSMM exposed to AHA with urea present in excess (500 mM). Enzyme structures are extracted from RCSB PDB (see Supplementary Note 3). f Average speed of UR-HSMM, extracted from the MSD analysis, and enzymatic activity for different AHA concentrations with urea present in excess (500 mM). Inset: correlation between speed of UR-HSMM and its enzymatic activity depending on inhibition. g Average speeds of UR-HSMM for different concentrations of AHA. Inset: average MSD of UR-HSMM exposed to AHA. Results are shown as the mean ± s.e.m. Twenty particles were analyzed per condition. Source data are provided as a Source Data file
