Key result
Measurements of actin binding indicated that the two heads of heavy meromyosin do not bind independently in the rigor complex, suggesting negative cooperativity or steric inhibition.
Population
In vitro model (fluorescently labeled heavy meromyosin and F-actin)
Comparison
Varying protein concentrations, temperature, KCl… vs Myosin subfragment I
Design
Preclinical
Authors
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Challenges independent myosin head binding models; leaves open cooperative effects on cardiac force generation.
The two heads of heavy meromyosin do not bind independently in the rigor complex, suggesting actin-transmitted negative cooperativity or steric inhibition.
Stefan Highsmith (1978) studied this question. Heavy meromyosin (HMM) vs. Myosin subfragment I was evaluated on Association of fluorescently labeled HMM and F-actin. Measurements of actin binding indicated that the two heads of heavy meromyosin do not bind independently in the rigor complex, suggesting negative cooperativity or steric inhibition.
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