Fig. 6: Effect of AmBleb on single molecule ATPase. | Communications Biology

Fig. 6: Effect of AmBleb on single molecule ATPase.

From: Single molecule turnover of fluorescent ATP by myosin and actomyosin unveil elusive enzymatic mechanisms

Fig. 6

a The molecular structure of para-aminoblebbistatin (AmBleb) is shown39. b Concentration–response curve for effect of AmBleb on sliding velocity at 60 mM ionic strength (1 mM MgATP) is shown using HMM. c Representative time traces of single molecule basal HMM ATPase without (i) or with 40 µM AmBleb (ii). Note two long dwell time events as direct consequence of effect of AmBleb on basal ATPase activity. d Cumulative dwell time distributions (i) of basal HMM ATPase in the absence and presence of 40 µM AmBleb were best fitted to double (control, data from 19 HMM molecules, Ndwell = 318) or triple (AmBleb, data from 31 HMM molecules, Ndwell = 280) exponential functions revealing an additional slow phase (ii, iii) with rate constant 0.006 s−1 (~8%) in the presence of AmBleb. Error estimates refer to 95% confidence intervals derived in the regression analysis. Temperature: 20 °C.

Back to article page