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. 2021 Jun 11;118(24):e2025030118. doi: 10.1073/pnas.2025030118

Table 1.

Parameters measured for β-cardiac myosin sS1

k0, s−1 δ, nm d, nm kcat, s−1 Kapp, μM V, nm⋅s−1 pCa50 n
WT 104 ± 10 1.39 ± 0.06 5.2 ± 0.3 4.1 ± 0.4 33 ± 6 762 ± 16 6.46 ± 0.04 2.2 ± 0.2
P710R 87 ± 5 0.31 ± 0.03**** 1.9 ± 0.3**** 2.5 ± 0.1* 14 ± 1* 239 ± 9**** 6.48 ± 0.07 3.1 ± 0.6

The rate of detachment from actin at zero load k0, its force sensitivity δ, and myosin’s step size d were measured from single molecules using the HFS technique (8 WT and 13 P710R molecules). kcat and Kapp were measured using a colorimetric actin-activated ATPase assay and were previously reported (29). Unloaded motility velocities V were measured by the motility assay with actin filaments (nine WT and eight P710R independent experiments). Calcium sensitivity parameters pCa50 and Hill coefficient n were measured by motility assay with regulated thin filaments (five WT and four P710R independent experiments). Data are presented as mean ± SEM. *P < 0.05 and ****P < 0.0001 different between P710R and WT.