Key result
Myosin subfragment-1 interacts tightly in rapid equilibrium with one and two G-actin molecules in the absence of ATP, forming binary GS and ternary G2S complexes (K > 10(7) M-1).
Population
G-actin and myosin subfragment-1 (S1) molecules
Comparison
Interaction in low ionic strength buffer and in… vs Interaction in the presence of ATP or ADP
Design
Preclinical
Authors
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Hypothesis-generating for rigor-state modeling in cardiac muscle; leaves open relevance to human contractility disorders.
Myosin subfragment-1 can form tight binary and ternary complexes with G-actin in the absence of ATP, suggesting a potential structural similarity to the F-acto-S1 complex in the rigor state.
Valentin-Ranc et al. (1991) studied this question. Myosin subfragment-1 was evaluated on Interaction between G-actin and myosin subfragment-1. Myosin subfragment-1 interacts tightly in rapid equilibrium with one and two G-actin molecules in the absence of ATP, forming binary GS and ternary G2S complexes (K > 10(7) M-1).
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