{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84211"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84211","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Investigating Ligand Induced Conformational Changes in the Estrogen Receptor","abstract":"Primarily, we have investigated ER conformational structure using the reporter group method of site-directed spin labeling (SDSL), along with electron paramagnetic resonance (EPR) spectroscopy. In this work, B and C parameter calculations from EPR line-shape theory express receptor differences quantitatively as a spectrum of conformational change. Relative squared difference (RSD) analysis allows us to compare ligand receptor complexes to one another. Furthermore, a rigorous statistical analysis shows that these measurements are reproducible. Placed in context, our work helps further the development of SDSL for the examination of protein conformation, and adds significantly to the hypothesis that the ER exists in a series of dynamic conformational forms depending upon the identity of bound ligand.","abstract_html":"Primarily, we have investigated ER conformational structure using the reporter group method of site-directed spin labeling (SDSL), along with electron paramagnetic resonance (EPR) spectroscopy. In this work, B and C parameter calculations from EPR line-shape theory express receptor differences quantitatively as a spectrum of conformational change. Relative squared difference (RSD) analysis allows us to compare ligand receptor complexes to one another. Furthermore, a rigorous statistical analysis shows that these measurements are reproducible. Placed in context, our work helps further the development of SDSL for the examination of protein conformation, and adds significantly to the hypothesis that the ER exists in a series of dynamic conformational forms depending upon the identity of bound ligand.","abstract_has_math":false,"creators":["Hurth, Kyle Marran"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Katzenellenbogen, John A."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:13:30Z","date_published":"2015-09-25T22:13:30Z","updated_at":"2026-07-22T22:26:22Z","subjects":["Biophysics, General"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3202106"],"render_values":[{"text":"(MiAaPQ)AAI3202106","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84211","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Katzenellenbogen, John A."]},{"key":"dc:creator","label":"Author","values":["Hurth, Kyle Marran"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:13:30Z","10000-01-01","2005"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biophysics, General"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/84211","(MiAaPQ)AAI3202106"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Primarily, we have investigated ER conformational structure using the reporter group method of site-directed spin labeling (SDSL), along with electron paramagnetic resonance (EPR) spectroscopy. 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