The sigmoidal form of the binding curves obtained [L. E. Greene and E. Eisenberg (1980) Proc. Nat. Acad. Sci. USA 77, 2616-2620] for the interaction of myosin subfragment 1 with regulated filaments is reinterpreted and shown to be consistent with a steric blocking model of muscle relaxation in which the interaction of tropomyosin with the myosin-binding sites on the actin filaments is considered to be an equilibrium process rather than an all-or-none phenomenon. Such an interpretation of the results has the advantage that dependence of the binding curve upon filament concentration is predicted, the previous models based on filament isomerization being deficient in this regard
ABSTRACTThe model of myosin regulation by a continuous tropomyosin chain is generalized to a chain o...
Contraction of striated muscles is regulated by tropomyosin strands that run continuously along acti...
The interaction between actin and myosin in the filament array of glycerinated muscle fibers has bee...
ABSTRACTWe present a model for cooperative myosin binding to the regulated actin filament, where tro...
ABSTRACT It was previously shown that a one-dimensional Ising model could successfully simulate the ...
Equilibrium titrations and kinetic experiments were used to define the cooperative binding of myosin...
The regulation of striated muscle contraction involves changes in the interactions of troponin and t...
AbstractIt was previously shown that a one-dimensional Ising model could successfully simulate the e...
A one-dimensional kinetic Ising model is developed to describe the binding of myosin subfragment 1 (...
The regulation of striated muscle contraction involves changes in the interactions of troponin and t...
Contraction of muscle involves the cyclic interaction of myosin heads on the thick filaments with ac...
Contraction of skeletal and cardiac muscle is controlled by Ca2+ ions via regulatory proteins, tropo...
A model has been developed for characterizing the interaction between strongly-binding myosin cross-...
<div><p>Muscle contracts due to ATP-dependent interactions of myosin motors with thin filaments comp...
Actin thin filaments containing bound tropomyosin (Tm) or tropomyosin troponin (Tm.Tn) exist in two ...
ABSTRACTThe model of myosin regulation by a continuous tropomyosin chain is generalized to a chain o...
Contraction of striated muscles is regulated by tropomyosin strands that run continuously along acti...
The interaction between actin and myosin in the filament array of glycerinated muscle fibers has bee...
ABSTRACTWe present a model for cooperative myosin binding to the regulated actin filament, where tro...
ABSTRACT It was previously shown that a one-dimensional Ising model could successfully simulate the ...
Equilibrium titrations and kinetic experiments were used to define the cooperative binding of myosin...
The regulation of striated muscle contraction involves changes in the interactions of troponin and t...
AbstractIt was previously shown that a one-dimensional Ising model could successfully simulate the e...
A one-dimensional kinetic Ising model is developed to describe the binding of myosin subfragment 1 (...
The regulation of striated muscle contraction involves changes in the interactions of troponin and t...
Contraction of muscle involves the cyclic interaction of myosin heads on the thick filaments with ac...
Contraction of skeletal and cardiac muscle is controlled by Ca2+ ions via regulatory proteins, tropo...
A model has been developed for characterizing the interaction between strongly-binding myosin cross-...
<div><p>Muscle contracts due to ATP-dependent interactions of myosin motors with thin filaments comp...
Actin thin filaments containing bound tropomyosin (Tm) or tropomyosin troponin (Tm.Tn) exist in two ...
ABSTRACTThe model of myosin regulation by a continuous tropomyosin chain is generalized to a chain o...
Contraction of striated muscles is regulated by tropomyosin strands that run continuously along acti...
The interaction between actin and myosin in the filament array of glycerinated muscle fibers has bee...