Key result
Binding of AdoPP[NH]P or trapping of ADP by orthovanadate shifts the thermal transition maximum of myosin subfragment 1 from 47.2°C to 53.2°C and 56.1°C, respectively, indicating two main conformations.
Population
Myosin subfragment 1 (S1) from rabbit skeletal muscles
Comparison
Binding of nucleotides vs Nucleotide-free S1
Design
Preclinical
Authors
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Provides no immediate clinical guidance; leaves open relevance of these conformations to human cardiac contractility.
The S1 molecule can exist in two main conformations corresponding to different states during ATP hydrolysis, as evidenced by changes in thermostability upon nucleotide binding.
Levitsky et al. (1992) studied Myosin subfragment 1 thermal unfolding. Nucleotide binding (AdoPP[NH]P, ADP-Vi, ADP) vs. Nucleotide-free S1 was evaluated on Thermal transition maximum and domain structure. Binding of AdoPP[NH]P or trapping of ADP by orthovanadate shifts the thermal transition maximum of myosin subfragment 1 from 47.2°C to 53.2°C and 56.1°C, respectively, indicating two main conformations.
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