The effects of force on actin-myosin ATPase activity

When skeletal and cardiac muscle contract they generate movement through the actin-myosin ATPase reaction. However, the chemical reaction underlying movement remains unclear. Specifically, little is known about how the forces generated by muscle influence the chemistry of the force-generating reaction. We measured the effects of mechanical forces on the actin-myosin ATPase activity using a standard motility assay and analysis for skeletal and cardiac muscle myosin. A mechanical load was imposed on a sliding actin filaments using alpha-actinin, and the corresponding effects of load were determined using a novel experimental and theoretical protocol. Our results show that mechanical loads decrease both actin-myosin attachment and detachment kinetics during actin sliding in skeletal and cardiac muscle, providing further insight into the mechanics of muscle contraction.

Name thesis:degree_name

Biochem and Molecular Biology

Level thesis:degree_level

Honors Thesis

Grantor

University of Nevada, Reno

Year dc:date.issued

2017

Author dc:creator

• Latham-Kapitz, Madison

Advisor dc:contributor.advisor

• Baker, Josh E.

Statement dc:rights

• Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 United States

Language dc:language.iso

en_US, English

Handle dc:identifier.uri

http://hdl.handle.net/11714/1923

OAI identifier oai:identifier

oai:scholarwolf.unr.edu:11714/1923