Recent theoretical work on the cooperative equilibrium binding of myosin subfragment-1-ADP to regulated actin, as influenced by Ca2+, is extended here to the cooperative steady-state ATPase activity of myosin subfragment-1 on regulated actin. Exact solution of the general steady-state problem will require Monte Carlo calculations. Three interrelated special cases are discussed in some detail and sample computer (not Monte Carlo) solutions are given. The eventual objective is to apply these considerations to in vitro experimental data and to in vivo muscle models
To treat the kinetics of actin-myosin binding as simply as possible, a one-variable model is develop...
Modeling the complete actin.myosin ATPase cycle has always been limited by the lack of experimental ...
© 2017 Biophysical Society Modeling the complete actin.myosin ATPase cycle has always been limited b...
Recent theoretical work on the cooperative equilibrium binding of myosin subfragment-1-ADP to regula...
It is shown by use of an extremely simple explicit two-state model that two basic ideas may be suffi...
A one-dimensional kinetic Ising model is developed to describe the binding of myosin subfragment 1 (...
AbstractSkeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tro...
Biochemical schemes for the actomyosin ATPase cycle as well as the cooperative regulation of ATPase ...
ABSTRACTWe present a model for cooperative myosin binding to the regulated actin filament, where tro...
Skeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tropomyosin...
AbstractThe regulation of muscle contraction by calcium involves interactions among actin filaments,...
The binding of actin to myosin subfragment 1 (S1) has been shown to occur as a two-step reaction. In...
Equilibrium titrations and kinetic experiments were used to define the cooperative binding of myosin...
ABSTRACT Skeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tr...
The actomyosin ATPase activity of skeletal myosin subfragment-1 (S-1) is typically studied by keepin...
To treat the kinetics of actin-myosin binding as simply as possible, a one-variable model is develop...
Modeling the complete actin.myosin ATPase cycle has always been limited by the lack of experimental ...
© 2017 Biophysical Society Modeling the complete actin.myosin ATPase cycle has always been limited b...
Recent theoretical work on the cooperative equilibrium binding of myosin subfragment-1-ADP to regula...
It is shown by use of an extremely simple explicit two-state model that two basic ideas may be suffi...
A one-dimensional kinetic Ising model is developed to describe the binding of myosin subfragment 1 (...
AbstractSkeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tro...
Biochemical schemes for the actomyosin ATPase cycle as well as the cooperative regulation of ATPase ...
ABSTRACTWe present a model for cooperative myosin binding to the regulated actin filament, where tro...
Skeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tropomyosin...
AbstractThe regulation of muscle contraction by calcium involves interactions among actin filaments,...
The binding of actin to myosin subfragment 1 (S1) has been shown to occur as a two-step reaction. In...
Equilibrium titrations and kinetic experiments were used to define the cooperative binding of myosin...
ABSTRACT Skeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tr...
The actomyosin ATPase activity of skeletal myosin subfragment-1 (S-1) is typically studied by keepin...
To treat the kinetics of actin-myosin binding as simply as possible, a one-variable model is develop...
Modeling the complete actin.myosin ATPase cycle has always been limited by the lack of experimental ...
© 2017 Biophysical Society Modeling the complete actin.myosin ATPase cycle has always been limited b...