Key result
Aging or oxidative modification causes a decrease in the fraction of myosins in the strong-binding state, which can be traced to the actin-binding cleft of the myosin catalytic domain.
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Electron paramagnetic resonance demonstrates that aging and oxidative stress alter actomyosin structural dynamics, reducing the fraction of myosins in the strong-binding state.
In Brief We have used site-directed spin labeling and electron paramagnetic resonance (EPR) to explore the effects of oxidation on muscle function, with particular focus on the actin-myosin interaction. EPR measurements show that aging or oxidative modification causes a decrease in the fraction of myosins in the strong-binding state, which can be traced to the actin-binding cleft of the myosin catalytic domain. Changes in actomyosin structural dynamics with aging and oxidative modification are resolved by electron paramagnetic resonance.
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Moen et al. (2013) studied Oxidative stress on muscle proteins. Aging or oxidative modification was evaluated on Fraction of myosins in the strong-binding state. Aging or oxidative modification causes a decrease in the fraction of myosins in the strong-binding state, which can be traced to the actin-binding cleft of the myosin catalytic domain.
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