Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins

Rebecca J. Moen; Jennifer C. Klein; David D. Thomas

doi:10.1249/JES.0000000000000004

Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins

Rebecca J. Moen, Jennifer C. Klein, David D. Thomas

Chemical and Structural Biology (TMED)

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	30-36
Number of pages	7
Journal	Exercise and sport sciences reviews
Volume	42
Issue number	1
DOIs	https://doi.org/10.1249/JES.0000000000000004
State	Published - Jan 2014

Keywords

ROS
actin
aging
methionine
muscle
myosin
reactive oxygen species

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AU - Thomas, David D.

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AB - 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.

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KW - actin

KW - aging

KW - methionine

KW - muscle

KW - myosin

KW - reactive oxygen species

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Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins

Abstract

Keywords

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