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Biophys J, December 2001, p. 3146-3155, Vol. 81, No. 6
Cavendish Laboratory, Madingley Road, Cambridge CB3 0HE, United Kingdom
We discuss a theoretical model for the cooperative
binding dynamics of tropomyosin to actin filaments. Tropomyosin binds
to actin by occupying seven consecutive monomers. The model includes a
strong attraction between attached tropomyosin molecules. We start with
an empty lattice and show that the binding goes through several stages.
The first stage represents fast initial binding and leaves many small
vacancies between blocks of bound molecules. In the second stage the
vacancies annihilate slowly as tropomyosin molecules detach and
reattach. Finally, the system approaches equilibrium. Using a
grain-growth model and a diffusion-coagulation model we give analytical
approximations for the vacancy density in all regimes.
Biophys J, December 2001, p. 3146-3155, Vol. 81, No. 6
© 2001 by the Biophysical Society 0006-3495/01/12/3146/10 $2.00
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