Event Title

Oxidative Effects on Muscle Protein Function

Location

CSU Ballroom

Start Date

21-4-2014 10:00 AM

End Date

21-4-2014 11:30 AM

Student's Major

Chemistry and Geology

Student's College

Science, Engineering and Technology

Mentor's Name

Rebecca Moen

Mentor's Email Address

rebecca.moen@mnsu.edu

Mentor's Department

Chemistry and Geology

Mentor's College

Science, Engineering and Technology

Description

Oxidative stress decreases muscle’s ability to produce force by specifically altering myosin, the main contractile protein in muscle, and is associated with muscle aging as well as various muscle diseases. The molecular mechanism responsible for myosin’s functional perturbations due to oxidation remains unclear. Purified myosin samples were treated with hydrogen peroxide to induce oxidative modifications at specific amino acid residues within the myosin catalytic domain. Myosin’s ability to hydrolyze ATP and bind actin was measured. Changes in myosin structural dynamics were monitored using electron paramagnetic resonance spectroscopy (EPR). Oxidation perturbs actomyosin functional interaction and produces a change in myosin’s structure, specifically impairing the weak-to-strong transition of myosin necessary for force production. As myosin is the molecular motor that drives muscle contraction, myosin is likely one of the main targets of site-specific amino acid oxidative modification induced by oxidative stress. These modifications of myosin cause contractile dysfunction leading to a decreased ability of muscle to produce force.

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Apr 21st, 10:00 AM Apr 21st, 11:30 AM

Oxidative Effects on Muscle Protein Function

CSU Ballroom

Oxidative stress decreases muscle’s ability to produce force by specifically altering myosin, the main contractile protein in muscle, and is associated with muscle aging as well as various muscle diseases. The molecular mechanism responsible for myosin’s functional perturbations due to oxidation remains unclear. Purified myosin samples were treated with hydrogen peroxide to induce oxidative modifications at specific amino acid residues within the myosin catalytic domain. Myosin’s ability to hydrolyze ATP and bind actin was measured. Changes in myosin structural dynamics were monitored using electron paramagnetic resonance spectroscopy (EPR). Oxidation perturbs actomyosin functional interaction and produces a change in myosin’s structure, specifically impairing the weak-to-strong transition of myosin necessary for force production. As myosin is the molecular motor that drives muscle contraction, myosin is likely one of the main targets of site-specific amino acid oxidative modification induced by oxidative stress. These modifications of myosin cause contractile dysfunction leading to a decreased ability of muscle to produce force.

Recommended Citation

Soboleva, Tatiana. "Oxidative Effects on Muscle Protein Function." Undergraduate Research Symposium, Mankato, MN, April 21, 2014.
http://cornerstone.lib.mnsu.edu/urs/2014/poster_session_A/6