{"id":{"repo_id":"unr","oai_identifier":"oai:scholarwolf.unr.edu:11714/1923"},"canonical_url":"https://search.dev.ndltd.org/etd/unr/oai:scholarwolf.unr.edu:11714/1923","repository":{"repo_id":"unr","name":"University of Nevada - Reno","base_url":"https://scholarwolf.unr.edu/server/oai/request"},"display":{"title":"The effects of force on actin-myosin ATPase activity","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.","abstract_html":"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_has_math":false,"creators":["Latham-Kapitz, Madison"],"institution":"University of Nevada, Reno","degree_name":"Biochem and Molecular Biology","degree_level":"Honors Thesis","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Baker, Josh E."],"committee_chairs":[],"committee_members":[],"year":2017,"date_issued":"2017","date_published":"2017","updated_at":"2026-07-27T21:47:25Z","subjects":[],"languages":["en_US","English"],"rights":["Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 United States"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/11714/1923","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Baker, Josh E."]},{"key":"dc:creator","label":"Author","values":["Latham-Kapitz, Madison"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2017-08-31T21:17:43Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2017-08-31T21:17:43Z"]},{"key":"dc:date.issued","label":"Date","values":["2017"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Honors Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Biochem and Molecular Biology"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Nevada, Reno"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]},{"key":"dc:language.iso","label":"Language (ISO)","values":["en_US"]},{"key":"dc:rights","label":"Dc Rights","values":["Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 United States"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/11714/1923"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The University of Nevada, Reno Libraries will promptly respond to removal requests related to content that violates intellectual property laws, data protections, or has been uploaded without creator consent. Takedown notices should be directed to our ScholarWolf team (scholarwolf@library.unr.edu) with information about the object, including its full URL and the nature of your complaint."]},{"key":"dc:description.abstract","label":"Abstract","values":["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."]},{"key":"dc:format","label":"Dc Format","values":["PDF"]},{"key":"dc:title","label":"Title","values":["The effects of force on actin-myosin ATPase activity"]}]}],"canonical_facts":{"dc:contributor.advisor":["Baker, Josh E."],"dc:creator":["Latham-Kapitz, Madison"],"dc:date.accessioned":["2017-08-31T21:17:43Z"],"dc:date.available":["2017-08-31T21:17:43Z"],"dc:date.issued":["2017"],"dc:description":["The University of Nevada, Reno Libraries will promptly respond to removal requests related to content that violates intellectual property laws, data protections, or has been uploaded without creator consent. Takedown notices should be directed to our ScholarWolf team (scholarwolf@library.unr.edu) with information about the object, including its full URL and the nature of your complaint."],"dc:description.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."],"dc:format":["PDF"],"dc:identifier.uri":["http://hdl.handle.net/11714/1923"],"dc:language":["English"],"dc:language.iso":["en_US"],"dc:rights":["Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 United States"],"dc:title":["The effects of force on actin-myosin ATPase activity"],"dc:type":["Thesis"],"thesis:degree_level":["Honors Thesis"],"thesis:degree_name":["Biochem and Molecular Biology"],"thesis:institution_name":["University of Nevada, Reno"]},"updated_at":"2026-07-27T21:47:25Z"}