{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84921"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84921","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Structural Characterization of the Amino- and Carboxy -Terminal Domains of Troponin C by High Pressure Nuclear Magnetic Resonance","abstract":"Our main research objective is to investigate the effects of high pressure on the structure, stability, and dynamics of proteins. The application of pressure provides a unique method to reversibly unfold proteins. Pressure is a gentler method of denaturation than other more traditional methods and also has the added benefit of generating a more concise thermodynamic description of the system. In our lab, one- and two-dimensional proton nuclear magnetic resonance is utilized to observe pressure-induced conformational changes and to isolate possible folding intermediates in proteins. Other techniques, such as computer simulations, circular dichroism, and fluorescence, are also utilized to obtain additional information. Through the use of a variety of spectroscopic techniques, the stability and folding pathways of proteins can be characterized.","abstract_html":"Our main research objective is to investigate the effects of high pressure on the structure, stability, and dynamics of proteins. The application of pressure provides a unique method to reversibly unfold proteins. Pressure is a gentler method of denaturation than other more traditional methods and also has the added benefit of generating a more concise thermodynamic description of the system. In our lab, one- and two-dimensional proton nuclear magnetic resonance is utilized to observe pressure-induced conformational changes and to isolate possible folding intermediates in proteins. Other techniques, such as computer simulations, circular dichroism, and fluorescence, are also utilized to obtain additional information. Through the use of a variety of spectroscopic techniques, the stability and folding pathways of proteins can be characterized.","abstract_has_math":false,"creators":["Yu, Aimee Cu"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Jonas, Ana","Jonas, Jiri"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:28:31Z","date_published":"2015-09-25T22:28:31Z","updated_at":"2026-07-22T22:26:24Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9990200"],"render_values":[{"text":"(MiAaPQ)AAI9990200","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84921","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Jonas, Ana","Jonas, Jiri"]},{"key":"dc:creator","label":"Author","values":["Yu, Aimee Cu"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:28:31Z","10000-01-01","2000"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"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":["Chemistry, Biochemistry"]}]},{"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/2142/84921","(MiAaPQ)AAI9990200"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Our main research objective is to investigate the effects of high pressure on the structure, stability, and dynamics of proteins. The application of pressure provides a unique method to reversibly unfold proteins. Pressure is a gentler method of denaturation than other more traditional methods and also has the added benefit of generating a more concise thermodynamic description of the system. In our lab, one- and two-dimensional proton nuclear magnetic resonance is utilized to observe pressure-induced conformational changes and to isolate possible folding intermediates in proteins. Other techniques, such as computer simulations, circular dichroism, and fluorescence, are also utilized to obtain additional information. Through the use of a variety of spectroscopic techniques, the stability and folding pathways of proteins can be characterized.","Made available in DSpace on 2015-09-25T22:28:31Z (GMT). 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The application of pressure provides a unique method to reversibly unfold proteins. Pressure is a gentler method of denaturation than other more traditional methods and also has the added benefit of generating a more concise thermodynamic description of the system. In our lab, one- and two-dimensional proton nuclear magnetic resonance is utilized to observe pressure-induced conformational changes and to isolate possible folding intermediates in proteins. Other techniques, such as computer simulations, circular dichroism, and fluorescence, are also utilized to obtain additional information. Through the use of a variety of spectroscopic techniques, the stability and folding pathways of proteins can be characterized.","Made available in DSpace on 2015-09-25T22:28:31Z (GMT). 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