The effects of force on actin-myosin ATPase activity
type: CreativeWork
description: 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.
abstract: 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.
author: Latham-Kapitz, Madison
language: en_US
language: English
date published: 2017
date modified: 2026-07-27T21:47:25Z
provider: University of Nevada - Reno
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Nevada, Reno

PropertyValue
property ID: Handle
value: http://hdl.handle.net/11714/1923