Table A1.
Parameter values of acto-myosin ATPase model
| Parameter | Value | Unit | Description | Reference |
|---|---|---|---|---|
| f01 | 1.2 | ms−1 | Rate constant from A⋅M⋅ADP⋅Pi to A⋅M⋅ADP | (27) a |
| g01min | 0.08 | mM−1 ms−1 | Minimum rate constant from A⋅M⋅ADP to A⋅M⋅ADP⋅Pi | (27) a |
| f1max | 0.005 | ms−1 | Maximum rate constant from M⋅ATP to A⋅M⋅ADP⋅Pi | |
| g1 | 0.05 | ms−1 | Rate constant from A⋅M⋅ADP⋅Pi to M⋅ATP | |
| f2 | 0.004 | ms−1 | Rate constant from A⋅M⋅ADP to A⋅M | |
| f3max | 0.9 | ms−1 | Maximum rate constant for A⋅M to M⋅ATP | |
| Km | 0.03 | mM | ATP half-saturation constant | (25) |
| Ki | 0.1 | mM | ADP inhibition constant | (26) |
| kltrpnp | 100 | ms−1 | Ca2+ on-rate for troponin low-affinity sites | (20) |
| kltrpnm | 4.0 × 10−2 | mM−1 ms−1 | Ca2+ off-rate for troponin low-affinity sites | (20) |
| [LTRPN]tot | 0.07 | mM | Total troponin low-affinity sites | |
| ζ | 0.1 | mM−1 kPa | Conversion factor normalizing to physiological force |
a
Parameters were doubled considering the temperature.