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. Author manuscript; available in PMC: 2017 Jan 12.
Published in final edited form as: Biochemistry. 2015 Dec 29;55(1):186–198. doi: 10.1021/acs.biochem.5b00817

Table 1.

1: Cardiac myosin actin-activated ATPase and in vitro motility

βmys
Δ0 NHD Δ17 @ 20% Δ17 @ 30% Δ17 @ 60% Δ17 MHD Δ17 HED
Vmax (s−1) 1.51±0.08 1.59±0.05 1.63±0.06 2.29±0.24 3.09±0.84 1.88±0.59
KM (µM) 9.33 ± 1.66 18.6±1.8 37.8±3.5 114.4± 20.6 - -
sm (µm/s) Qdot 0.27±0.02 - 0.29±0.02 0.32±0.03 0.40±0.04 0.25±0.04
sm (µm/s) standard 0.26±0.02 - 0.31±0.02 0.31±0.01 - -
<d> (nm) 6.0±0.3 - 6.2±0.4 5.7±0.5 6.1±0.5 5.5±0.5
<F> (uf) 14.4±1.2 - 16.8±1.6 19.6±2.3 24.1±2.0 21.7±2.6
<P> (µm/s) (uf) 3.9±0.3 - 4.4±0.4 6.3±0.7 9.7±0.5 5.5±0.3
αmys
NTg NHD WT @ 30% WT MHD Δ43 @ 60% Δ43 MHD
Vmax (s−1) 2.67±0.24 2.60±0.19 2.53±0.44 1.50±0.09 1.28±0.09
KM (µM) 3.55±1.08 3.18±0.80 - 4.35±0.85 -
sm (µm/s) Qdot 1.21±0.07 1.24±0.06 1.31±0.38 1.14±0.04 1.00±0.14
sm (µm/s) standard 1.02±0.06 0.97±0.08 - 0.82±0.04 -
<d> (nm) 6.9±0.4 6.0±0.3 6.0±2.4 6.2±0.4 6.2±0.4
<F> (uf) 6.6±0.7 5.5±0.7 4.9±1.4 3.8±0.3 3.6±0.5
<P> (µm/s) (uf) 8.0±0.9 6.8±0.9 6.5±2.0 4.4±0.4 3.7±0.2
1

Vmax and KM are defined in eq. S1 from SI. Motility velocity sm from standard and Qdot motility assays occasionally differ for the higher velocity αmys because subtraction of thermal/mechanical fluctuations, possible only with Qdot data, removes some of the lowest velocities in the velocity histogram that are not due to myosin activity. This effect is negligible for βmys. Quantities denoted by <q> are ensemble averages defined in System (ensemble) analytics (Section B. SI) for step-size, d, force F, and power, P. Average force <F> is in arbitrary units of force (uf). All experimental errors indicated are standard deviation. Quantities for the MHD and HED pure species are calculated using eqs. 1 & 7 as explained in Methods with standard deviation estimated by random variate generation from their probability distribution as described (45).