Key result
The addition of nucleotides such as ADP, AMP-P(NH)P, and PPi affected the binding of myosin subfragment 1 and F-actin, with ADP yielding an interaction free energy of -4.67 kJ M-1.
Population
Myosin subfragment 1 (S-1) and pure F-actin (A)
Design
Preclinical
Authors
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Offers foundational actomyosin data; extends nucleotide-binding models but leaves clinical cardiac translation open.
The study maps the nucleotide binding site on myosin subfragment 1 with respect to its interaction on the actin binding site, demonstrating the existence of a ternary complex for ADP, S-1, and actin.
Stefan Highsmith (1976) studied this question. Nucleotides (ADP, AMP-P(NH)P, PPi) was evaluated on Binding of myosin subfragment 1 (S-1) and pure F-actin (A). The addition of nucleotides such as ADP, AMP-P(NH)P, and PPi affected the binding of myosin subfragment 1 and F-actin, with ADP yielding an interaction free energy of -4.67 kJ M-1.
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