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- W2058477002 abstract "Structural models based upon crystal structures show the myosin nucleotide-binding pocket closes around the ATP. EPR spectroscopy using nitroxide spin label covalently attached to ADP on the ribose moiety detects the degree of closure around this pocket. Our work with spin labeled nucleotide indicates that the pocket opens up in actomyosin, presumably to facilitate ADP release. Actomyosin spectra show evidence that the open and closed states are in equilibrium. Deconvolution of the spectra allows a quantitative analysis of this equilibrium yielding a ΔG for this structural transition. We have looked at this equilibrium in a range of different myosins, ranging from slow myosins such as myosin V and smooth muscle to faster myosins from skeletal muscle and Drosophila flight muscle. Assuming the open state is a necessary intermediate for ADP release, we have found a counterintuitive result that the closed state is favored in faster myosins and the open state is favored in slow myosin. The ΔG for the closed to open transition is proportional to the in vitro motility and the ADP affinity. The ability to observe the structural equilibrium gives an insight into the energetics of the actomyosin ADP state. We hypothesize that this correlation represents a destabilization of the open state in actomyosin ADP that results in a faster ADP release rate. Extending the analysis, the ΔG also correlates to muscle efficiency, which suggests that the energetics in this state play a central roll in the tradeoff between speed and efficiency in myosin." @default.
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- W2058477002 date "2009-02-01" @default.
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- W2058477002 title "Thermodynamics Of The Myosin Nucleotide-binding Pocket Measured By Epr Spectroscopy Using Spin Labeled Nucleotides" @default.
- W2058477002 doi "https://doi.org/10.1016/j.bpj.2008.12.1076" @default.
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