Faculty and Student Publications
Document Type
Article
Publication Date
5-4-2022
Abstract
Myosins are motor proteins that hydrolyze ATP to step along actin filament (AF) tracks and are essential in cellular processes such as motility and muscle contraction. To understand their force-generating mechanisms, myosin II has been investigated both at the single-molecule (SM) level and as teams of motors in vitro using biophysical methods such as optical trapping. These studies showed that myosin force-generating behavior can differ greatly when moving from the single-molecule level in a three-bead arrangement to groups of motors working together on a rigid bead or coverslip surface in a gliding arrangement. However, these assay constructions do not permit evaluating the group dynamics of myosin within viscoelastic structural hierarchy as they would within a cell. We have developed a method using optical tweezers to investigate the mechanics of force generation by myosin ensembles interacting with multiple actin filaments. These actomyosin bundles facilitate investigation in a hierarchical and compliant environment that captures motor communication and ensemble force output. The customizable nature of the assay allows for altering experimental conditions to understand how modifications to the myosin ensemble, actin filament bundle, or the surrounding environment result in differing force outputs.
Relational Format
journal article
Recommended Citation
Azzam, O. A., Watts, J. C., Reynolds, J. E., Davis, J. E., & Reinemann, D. N. (2022). Probing Myosin ensemble mechanics in Actin filament bundles using optical tweezers. Journal of Visualized Experiments, 183. https://doi.org/10.3791/63672
DOI
10.3791/63672
Accessibility Status
Searchable text
Included in
Biomedical Engineering and Bioengineering Commons, Chemical Engineering Commons, Civil and Environmental Engineering Commons, Computer Engineering Commons, Electrical and Computer Engineering Commons, Geological Engineering Commons, Mechanical Engineering Commons
