{"id":{"repo_id":"unt","oai_identifier":"info:ark/67531/metadc4514"},"canonical_url":"https://search.dev.ndltd.org/etd/unt/info:ark/67531/metadc4514","repository":{"repo_id":"unt","name":"University of North Texas","base_url":"https://digital.library.unt.edu/oai/"},"display":{"title":"Studies on actomyosin crossbridge flexibility using a new single molecule assay.","abstract":"Several key flexure sites exist in the muscle crossbridge including the actomyosin binding site which play important roles in the actomyosin crossbridge cycle. To distinguish between these sources of flexibility, a new single molecule assay was developed to observe the swiveling of rod about a single myosin. Myosins attached through a single crossbridge displayed mostly similar torsional characteristics compared to myosins attached through two crossbridges, which indicates that most of the torsional flexibility resides in the myosin subfragment-2, and thus the hinge between subfragment-2 and light meromyosin should contribute the most to this flexibility. The comparison of torsional characteristics in the absence and presence of ADP demonstrated a small but significant increase in twist rates for the double-headed myosins but no increase for single-headed myosins, which indicates that the ADP-induced increase in flexibility arises due to changes in the myosin head and verifies that most flexibility resides in myosin subfragment-2.","abstract_html":"Several key flexure sites exist in the muscle crossbridge including the actomyosin binding site which play important roles in the actomyosin crossbridge cycle. To distinguish between these sources of flexibility, a new single molecule assay was developed to observe the swiveling of rod about a single myosin. Myosins attached through a single crossbridge displayed mostly similar torsional characteristics compared to myosins attached through two crossbridges, which indicates that most of the torsional flexibility resides in the myosin subfragment-2, and thus the hinge between subfragment-2 and light meromyosin should contribute the most to this flexibility. The comparison of torsional characteristics in the absence and presence of ADP demonstrated a small but significant increase in twist rates for the double-headed myosins but no increase for single-headed myosins, which indicates that the ADP-induced increase in flexibility arises due to changes in the myosin head and verifies that most flexibility resides in myosin subfragment-2.","abstract_has_math":false,"creators":["Gundapaneni, Deepika"],"institution":"University of North Texas","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Root, Douglas D.","Chapman, Kent D.","Padilla, Pamela"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2004,"date_issued":"2004-05","date_published":"2004-05","updated_at":"2026-07-24T05:35:09Z","subjects":["Actomyosin.","torsional flexibility","actomyosin","crossbridge","single molecule assay","ADP"],"languages":["English"],"rights":["Public","Copyright","Gundapaneni, Deepika","Copyright is held by the author, unless otherwise noted. All rights reserved."],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["oclc: 55665751","https://digital.library.unt.edu/ark:/67531/metadc4514/","ark: ark:/67531/metadc4514"],"render_values":[{"text":"oclc: 55665751","href":null,"code":true},{"text":"https://digital.library.unt.edu/ark:/67531/metadc4514/","href":"https://digital.library.unt.edu/ark:/67531/metadc4514/","code":true},{"text":"ark: ark:/67531/metadc4514","href":null,"code":true}]}]},"links":{"outbound_url":"https://doi.org/10.12794/metadc4514","outbound_label":"DOI","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Root, Douglas D.","Chapman, Kent D.","Padilla, Pamela"]},{"key":"dc:creator","label":"Author","values":["Gundapaneni, Deepika"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2004-05"]},{"key":"dc:publisher","label":"Institution","values":["University of North Texas"]},{"key":"dc:type","label":"Dc Type","values":["Thesis or Dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Actomyosin.","torsional flexibility","actomyosin","crossbridge","single molecule assay","ADP"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]},{"key":"dc:rights","label":"Dc Rights","values":["Public","Copyright","Gundapaneni, Deepika","Copyright is held by the author, unless otherwise noted. 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Myosins attached through a single crossbridge displayed mostly similar torsional characteristics compared to myosins attached through two crossbridges, which indicates that most of the torsional flexibility resides in the myosin subfragment-2, and thus the hinge between subfragment-2 and light meromyosin should contribute the most to this flexibility. The comparison of torsional characteristics in the absence and presence of ADP demonstrated a small but significant increase in twist rates for the double-headed myosins but no increase for single-headed myosins, which indicates that the ADP-induced increase in flexibility arises due to changes in the myosin head and verifies that most flexibility resides in myosin subfragment-2."]},{"key":"dc:format","label":"Dc Format","values":["Text"]},{"key":"dc:title","label":"Title","values":["Studies on actomyosin crossbridge flexibility using a new single molecule assay."]}]}],"canonical_facts":{"dc:contributor":["Root, Douglas D.","Chapman, Kent D.","Padilla, Pamela"],"dc:creator":["Gundapaneni, Deepika"],"dc:date":["2004-05"],"dc:description":["Several key flexure sites exist in the muscle crossbridge including the actomyosin binding site which play important roles in the actomyosin crossbridge cycle. To distinguish between these sources of flexibility, a new single molecule assay was developed to observe the swiveling of rod about a single myosin. Myosins attached through a single crossbridge displayed mostly similar torsional characteristics compared to myosins attached through two crossbridges, which indicates that most of the torsional flexibility resides in the myosin subfragment-2, and thus the hinge between subfragment-2 and light meromyosin should contribute the most to this flexibility. The comparison of torsional characteristics in the absence and presence of ADP demonstrated a small but significant increase in twist rates for the double-headed myosins but no increase for single-headed myosins, which indicates that the ADP-induced increase in flexibility arises due to changes in the myosin head and verifies that most flexibility resides in myosin subfragment-2."],"dc:format":["Text"],"dc:identifier":["oclc: 55665751","doi: 10.12794/metadc4514","https://digital.library.unt.edu/ark:/67531/metadc4514/","ark: ark:/67531/metadc4514"],"dc:language":["English"],"dc:publisher":["University of North Texas"],"dc:rights":["Public","Copyright","Gundapaneni, Deepika","Copyright is held by the author, unless otherwise noted. 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