{"id":{"repo_id":"umn","oai_identifier":"oai:conservancy.umn.edu:11299/170672"},"canonical_url":"https://search.dev.ndltd.org/etd/umn/oai:conservancy.umn.edu:11299/170672","repository":{"repo_id":"umn","name":"University of Minnesota","base_url":"https://conservancy.umn.edu/server/oai/request"},"display":{"title":"Conformational changes in actinin-type actin binding domains: probing actin-induced structural dynamics in dystrophin and utrophin using EPR spectroscopy.","abstract":"The underlying cause of Duchenne and Becker muscular dystrophies is a lack of functional dystrophin, a large multidomain protein. Dystrophin is normally expressed in muscle, where it links the extracellular matrix to the cortical actin cytoskeleton via a complex of associated proteins. Dystrophin, and its autosomal homologue utrophin, connect with the actin cytoskeleton through two F-actin binding domains, including an N-terminal \"actinin-type\" actin binding domain (ABD).In addition to dystrophin and utrophin, actinin-type ABDs are found in a large number of proteins. Nonetheless, the actin binding mechanism remains poorly understood: x-ray crystallography and electron microscopy have produced conflicting models. Electron paramagnetic resonance (EPR) spectroscopy, especially double electron-electron resonance (DEER), can be used to distinguish between these models or to build new models. In this thesis, I present data from DEER experiments which suggest that actinin-type ABDs of dystrophin and utrophin adopt unexpected conformations in solution.","abstract_html":"The underlying cause of Duchenne and Becker muscular dystrophies is a lack of functional dystrophin, a large multidomain protein. Dystrophin is normally expressed in muscle, where it links the extracellular matrix to the cortical actin cytoskeleton via a complex of associated proteins. Dystrophin, and its autosomal homologue utrophin, connect with the actin cytoskeleton through two F-actin binding domains, including an N-terminal "actinin-type" actin binding domain (ABD).In addition to dystrophin and utrophin, actinin-type ABDs are found in a large number of proteins. Nonetheless, the actin binding mechanism remains poorly understood: x-ray crystallography and electron microscopy have produced conflicting models. Electron paramagnetic resonance (EPR) spectroscopy, especially double electron-electron resonance (DEER), can be used to distinguish between these models or to build new models. In this thesis, I present data from DEER experiments which suggest that actinin-type ABDs of dystrophin and utrophin adopt unexpected conformations in solution.","abstract_has_math":false,"creators":["Crain, Jonathan"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-12","date_published":"2014-12","updated_at":"2026-07-24T05:20:03Z","subjects":["Deer","Dystrophin","Utrophin","Biochemistry, molecular bio, and biophysics"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/11299/170672","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Crain, Jonathan"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2015-03-20T19:04:41Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2015-03-20T19:04:41Z"]},{"key":"dc:date.issued","label":"Date","values":["2014-12"]},{"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":["Deer","Dystrophin","Utrophin","Biochemistry, molecular bio, and biophysics"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/11299/170672"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["University of Minnesota M.S. thesis. December 2014. Major: Biochemistry, Molecular Bio, and Biophysics. Advisor: Dr. David D. Thomas. 1 computer file (PDF); vii, 29 pages."]},{"key":"dc:description.abstract","label":"Abstract","values":["The underlying cause of Duchenne and Becker muscular dystrophies is a lack of functional dystrophin, a large multidomain protein. Dystrophin is normally expressed in muscle, where it links the extracellular matrix to the cortical actin cytoskeleton via a complex of associated proteins. Dystrophin, and its autosomal homologue utrophin, connect with the actin cytoskeleton through two F-actin binding domains, including an N-terminal \"actinin-type\" actin binding domain (ABD).In addition to dystrophin and utrophin, actinin-type ABDs are found in a large number of proteins. Nonetheless, the actin binding mechanism remains poorly understood: x-ray crystallography and electron microscopy have produced conflicting models. Electron paramagnetic resonance (EPR) spectroscopy, especially double electron-electron resonance (DEER), can be used to distinguish between these models or to build new models. In this thesis, I present data from DEER experiments which suggest that actinin-type ABDs of dystrophin and utrophin adopt unexpected conformations in solution."]},{"key":"dc:title","label":"Title","values":["Conformational changes in actinin-type actin binding domains: probing actin-induced structural dynamics in dystrophin and utrophin using EPR spectroscopy."]}]}],"canonical_facts":{"dc:creator":["Crain, Jonathan"],"dc:date.accessioned":["2015-03-20T19:04:41Z"],"dc:date.available":["2015-03-20T19:04:41Z"],"dc:date.issued":["2014-12"],"dc:description":["University of Minnesota M.S. thesis. December 2014. Major: Biochemistry, Molecular Bio, and Biophysics. Advisor: Dr. David D. Thomas. 1 computer file (PDF); vii, 29 pages."],"dc:description.abstract":["The underlying cause of Duchenne and Becker muscular dystrophies is a lack of functional dystrophin, a large multidomain protein. Dystrophin is normally expressed in muscle, where it links the extracellular matrix to the cortical actin cytoskeleton via a complex of associated proteins. Dystrophin, and its autosomal homologue utrophin, connect with the actin cytoskeleton through two F-actin binding domains, including an N-terminal \"actinin-type\" actin binding domain (ABD).In addition to dystrophin and utrophin, actinin-type ABDs are found in a large number of proteins. Nonetheless, the actin binding mechanism remains poorly understood: x-ray crystallography and electron microscopy have produced conflicting models. Electron paramagnetic resonance (EPR) spectroscopy, especially double electron-electron resonance (DEER), can be used to distinguish between these models or to build new models. In this thesis, I present data from DEER experiments which suggest that actinin-type ABDs of dystrophin and utrophin adopt unexpected conformations in solution."],"dc:identifier.uri":["http://hdl.handle.net/11299/170672"],"dc:language.iso":["en"],"dc:subject":["Deer","Dystrophin","Utrophin","Biochemistry, molecular bio, and biophysics"],"dc:title":["Conformational changes in actinin-type actin binding domains: probing actin-induced structural dynamics in dystrophin and utrophin using EPR spectroscopy."],"dc:type":["Thesis or Dissertation"]},"updated_at":"2026-07-24T05:20:03Z"}