Key result
The affinity constant of the tropomyosin head-to-tail interaction changes by almost 2 orders of magnitude over an ionic strength range of 50 mM (between I = 0.045 and 0.095).
The affinity constant of tropomyosin head-to-tail interaction changes by almost 2 orders of magnitude over an ionic strength range of 50 mM, which is important for interpreting binding isotherms with actin and troponin.
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Strong ionic strength dependence of tropomyosin affinity warrants caution in interpreting in vitro binding data; leaves open its role in cardiac thin-filament regulation.
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Sousa et al. (2002) studied this question. Recombinant chicken α-tropomyosin with 5-hydroxytryptophan at position 269 was evaluated on Equilibrium constant of the head-to-tail interaction as a function of ionic strength. The affinity constant of the tropomyosin head-to-tail interaction changes by almost 2 orders of magnitude over an ionic strength range of 50 mM (between I = 0.045 and 0.095).
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