Event Title

Oxidative Effects on Muscle Protein Contractile Function

Location

CSU Ballroom

Start Date

20-4-2015 10:00 AM

End Date

20-4-2015 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

Muscle is made up of two main contractile proteins, myosin and actin. In this actomyosin complex, myosin is the molecular “motor” using the universal energy source adenosine triphosphate (ATP) to produce force and movement. At the molecular level, myosin undergoes a series of structural transitions upon force generation: an open-to-close transition of the actin-binding site, a close-toopen transition of the ATP binding site, and a rotation of the “lever arm”. Perturbations in the opento- close transition of myosin’s actin-binding cleft have been associated with both oxidation stress and muscle aging as well as various muscle diseases including muscular dystrophy and hypertrophic cardiomyopathies. This project focuses on one main hypothesis. I predict that myosin’s open-toclose transition of the actin-binding site is necessary for proper actomyosin function, for both actinactivated ATPase structural dynamics and actomyosin complex formation. Methodology: Crosslinking of the actin-binding cleft will be accomplished using the BSL. Control samples will include no spin-label and a monofunctionally attached spin-label. Actin’s ability to bind myosin and activate it will be tested via a myosin enzymatic activity assay. Pyrene-actin fluorescence quenching will be used to determine the ability to from strongly bound actomyosin complexes. Anticipated Outcomes: I anticipate there will be a change in the ability of myosin to bind actin which is partially responsible for myosin’s decreased ability to generate force. However, a lack of change could suggest significant changes in the binding-site availability for the substrate which could be the focus of future research.

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Apr 20th, 10:00 AM Apr 20th, 11:30 AM

Oxidative Effects on Muscle Protein Contractile Function

CSU Ballroom

Muscle is made up of two main contractile proteins, myosin and actin. In this actomyosin complex, myosin is the molecular “motor” using the universal energy source adenosine triphosphate (ATP) to produce force and movement. At the molecular level, myosin undergoes a series of structural transitions upon force generation: an open-to-close transition of the actin-binding site, a close-toopen transition of the ATP binding site, and a rotation of the “lever arm”. Perturbations in the opento- close transition of myosin’s actin-binding cleft have been associated with both oxidation stress and muscle aging as well as various muscle diseases including muscular dystrophy and hypertrophic cardiomyopathies. This project focuses on one main hypothesis. I predict that myosin’s open-toclose transition of the actin-binding site is necessary for proper actomyosin function, for both actinactivated ATPase structural dynamics and actomyosin complex formation. Methodology: Crosslinking of the actin-binding cleft will be accomplished using the BSL. Control samples will include no spin-label and a monofunctionally attached spin-label. Actin’s ability to bind myosin and activate it will be tested via a myosin enzymatic activity assay. Pyrene-actin fluorescence quenching will be used to determine the ability to from strongly bound actomyosin complexes. Anticipated Outcomes: I anticipate there will be a change in the ability of myosin to bind actin which is partially responsible for myosin’s decreased ability to generate force. However, a lack of change could suggest significant changes in the binding-site availability for the substrate which could be the focus of future research.

Recommended Citation

Soboleva, Tatiana. "Oxidative Effects on Muscle Protein Contractile Function." Undergraduate Research Symposium, Mankato, MN, April 20, 2015.
http://cornerstone.lib.mnsu.edu/urs/2015/poster_session_A/32