Liao et al. 10.1073/pnas.0611519104.

Supporting Information

Files in this Data Supplement:

SI Text
SI Figure 5
SI Figure 6
SI Table 1




Fig. 5. Six possible transitions of a double-headed myosin state. In this example, the original state is AMT-AMT, where both heads bind to actin with ATP in their individual catalytic sites. Either head can experience ATP hydrolysis and the state transits to either AMT-AMDP or AMDP-AMT. Either head can also release ATP and becomes either AMT-AM or AM-AMT. Another possibility is that either head can detach from the actin to reach state AMT-MT or MT-AMT.





Fig. 6. The kinetic scheme for a double-headed myosin expanded from Fig. 5. The whole kinetic network contains 64 states and 384 possible transitions.





Table 1. Rates for the kinetics of single-headed myosin

 

Forward rates

Backward rates

M↔MT

1.9x105 M-1s-1(2)

4.0x10-7 s-1

MT↔MDP

660.6 s-1(2)

89.4 s-1(2)

MDP↔MD

0.1 s-1(2)

0.1 M-1s-1(2)

MD↔MD*

0.1 s-1

0.1 s-1

MD*↔M

1.2 s-1(3)

4.79x106 M-1s-1(3)

AM↔AMT

2.4x106 M-1s-1

0.03 s-1

AMT↔AMDP

1.0 s-1

0.03 s-1

AMDP↔AMD

250 s-1(3)

9.0 M-1s-1

AMD↔AMD*

100 s-1

10.0 s-1

AMD*↔AM

13 s-1(3)

1.28x107 M-1s-1(3)

M↔AM

7.3x107 M-1s-1(3)

0.166 s-1(2)

MT↔AMT

8.0x107 M-1s-1

990 s-1

MDP↔AMDP

4.7x106 M-1s-1(3)

14.3 s-1(2)

MD↔AMD

1.4x107 M-1s-1

1.6 s-1

MD*↔AMD*

2.2x108 M-1s-1

2.0 s-1