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
Recent experiments on the kinetics of the interaction between myosin subfragment 1 (S1) and F-actin ...
The mechanics of the actomyosin interaction is central in muscle contraction and intracellular traff...
Regulation of skeletal muscle contraction is achieved through the interaction of six different prote...
Recent theoretical work on the cooperative equilibrium binding of myosin subfragment-1-ADP to regula...
Biochemical schemes for the actomyosin ATPase cycle as well as the cooperative regulation of ATPase ...
Skeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tropomyosin...
It is shown by use of an extremely simple explicit two-state model that two basic ideas may be suffi...
AbstractSkeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tro...
The actomyosin ATPase activity of skeletal myosin subfragment-1 (S-1) is typically studied by keepin...
ABSTRACT Skeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tr...
A one-dimensional kinetic Ising model is developed to describe the binding of myosin subfragment 1 (...
ABSTRACTWe present a model for cooperative myosin binding to the regulated actin filament, where tro...
The energy for muscle contraction is derived from the hydrolysis of ATP, and one of the principal pr...
We present Monte Carlo simulations for a molecular motor system found in virtually all eukaryotic ce...
© 2017 Biophysical Society Modeling the complete actin.myosin ATPase cycle has always been limited b...
Recent experiments on the kinetics of the interaction between myosin subfragment 1 (S1) and F-actin ...
The mechanics of the actomyosin interaction is central in muscle contraction and intracellular traff...
Regulation of skeletal muscle contraction is achieved through the interaction of six different prote...
Recent theoretical work on the cooperative equilibrium binding of myosin subfragment-1-ADP to regula...
Biochemical schemes for the actomyosin ATPase cycle as well as the cooperative regulation of ATPase ...
Skeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tropomyosin...
It is shown by use of an extremely simple explicit two-state model that two basic ideas may be suffi...
AbstractSkeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tro...
The actomyosin ATPase activity of skeletal myosin subfragment-1 (S-1) is typically studied by keepin...
ABSTRACT Skeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tr...
A one-dimensional kinetic Ising model is developed to describe the binding of myosin subfragment 1 (...
ABSTRACTWe present a model for cooperative myosin binding to the regulated actin filament, where tro...
The energy for muscle contraction is derived from the hydrolysis of ATP, and one of the principal pr...
We present Monte Carlo simulations for a molecular motor system found in virtually all eukaryotic ce...
© 2017 Biophysical Society Modeling the complete actin.myosin ATPase cycle has always been limited b...
Recent experiments on the kinetics of the interaction between myosin subfragment 1 (S1) and F-actin ...
The mechanics of the actomyosin interaction is central in muscle contraction and intracellular traff...
Regulation of skeletal muscle contraction is achieved through the interaction of six different prote...