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. Author manuscript; available in PMC: 2013 Mar 16.
Published in final edited form as: J Mol Biol. 2012 Jan 28;417(1-2):112–128. doi: 10.1016/j.jmb.2012.01.011

Table 2.

Estimated parameters of the Hill model from the best fits of stopped flow data (for both excess [S1] and excess [actin]) and titrations at pCa 8.9. The comparison contrasts the estimated parameters for prescribed reverse constants k−1 = 500 s−1 and Y2 =0.208 reported in Chen at al.1 at high [Ca2+] and used in all our simulations (denoted as “High Ca2+ Rev. R.C.”) vs. the reverse constants k−1 =0.6 s−1 and Y2 = 0.0703 reported in1 at low [Ca2+] (denoted as “Low. Ca2+ Rev. R.C.”).

Stopped Flow Titrations

Excess Actin Excess Myosin High Ca2+ Rev. R.C. Low Ca2+ Rev. R.C.
High Ca2+ Rev. R.C. Low Ca2+ Rev. R.C. High Ca2+ Rev. R.C. Low Ca2+ Rev. R.C.
αo 82.3 200 81 200 200 200
βo 300 300 300 300 300 300
Y1 5.576 15.27 7.149 18.2 78.0 52.0
Y2 0.208 0.0703 0.208 0.0703 0.2080 0.0703
k1 2.29 0.6 1.7 0.6 18 0.6
k−1 500 3.0 500 3.0 500 3.0
k2 1.761 3.50 1.207 0.95 7.00 7.00
k−2 0.09 0.09 0.09 0.09 0.09 0.09
γ 0.8 0.8 0.8 0.8 0.8 0.8
δ 0.5 0.5 0.5 0.5 0.5 0.5
K1 0.0046 0.200 0.0034 0.200 0.036 0.200
K2 19.57 38.89 13.42 10.56 77.78 77.78
Y 1.160 1.073 1.487 1.279 16.224 3.656
L′ 98 145 127 173 250 493

k1 and k2 have units of μM−1s−1; K1 and K2, have units of μM−1; equilibrium constants Y and L′, and cooperativity parameters Y1, Y2, γ and δ are dimensionless; all other rate constants have units of s−1.