{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84153"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84153","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Development of High Pressure Surface Plasmon Resonance for the Study of Biosystems","abstract":"Through an initial set of experiments high pressure SPR (HP-SPR) was used to measure changes in the reflectivity of various liquids under hydrostatic pressures ranging from ambient to 276 bar (4000 psi). The changes in refractive index as a function of increasing pressure for these solutions were compared and an indication of how these methods can be used to determine volume changes in biomolecular interactions is provided. The application of HP-SPR was extended to the use of commercially available sensor chips. We have shown that BIAcore(TM) SA chips maintain their surface binding functionality after pressure exposure and that effects to the surface are reversible to 6000 psi. Three test systems were chosen to be studied using this instrument, each having different characteristics; cytochrome c association to cytochrome b5, unfolding of staphylococcal nuclease, and binding of the BamH1 restriction enzyme to its DNA recognition site.","abstract_html":"Through an initial set of experiments high pressure SPR (HP-SPR) was used to measure changes in the reflectivity of various liquids under hydrostatic pressures ranging from ambient to 276 bar (4000 psi). The changes in refractive index as a function of increasing pressure for these solutions were compared and an indication of how these methods can be used to determine volume changes in biomolecular interactions is provided. The application of HP-SPR was extended to the use of commercially available sensor chips. We have shown that BIAcore(TM) SA chips maintain their surface binding functionality after pressure exposure and that effects to the surface are reversible to 6000 psi. Three test systems were chosen to be studied using this instrument, each having different characteristics; cytochrome c association to cytochrome b5, unfolding of staphylococcal nuclease, and binding of the BamH1 restriction enzyme to its DNA recognition site.","abstract_has_math":false,"creators":["Kelley, Jennifer Gann"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Sligar, Stephen G."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:13:13Z","date_published":"2015-09-25T22:13:13Z","updated_at":"2026-07-22T22:26:22Z","subjects":["Chemistry, Analytical"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3153349"],"render_values":[{"text":"(MiAaPQ)AAI3153349","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84153","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Sligar, Stephen G."]},{"key":"dc:creator","label":"Author","values":["Kelley, Jennifer Gann"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:13:13Z","10000-01-01","2004"]},{"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":["Chemistry, Analytical"]}]},{"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/2142/84153","(MiAaPQ)AAI3153349"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Through an initial set of experiments high pressure SPR (HP-SPR) was used to measure changes in the reflectivity of various liquids under hydrostatic pressures ranging from ambient to 276 bar (4000 psi). The changes in refractive index as a function of increasing pressure for these solutions were compared and an indication of how these methods can be used to determine volume changes in biomolecular interactions is provided. The application of HP-SPR was extended to the use of commercially available sensor chips. We have shown that BIAcore(TM) SA chips maintain their surface binding functionality after pressure exposure and that effects to the surface are reversible to 6000 psi. Three test systems were chosen to be studied using this instrument, each having different characteristics; cytochrome c association to cytochrome b5, unfolding of staphylococcal nuclease, and binding of the BamH1 restriction enzyme to its DNA recognition site.","Made available in DSpace on 2015-09-25T22:13:13Z (GMT). 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The changes in refractive index as a function of increasing pressure for these solutions were compared and an indication of how these methods can be used to determine volume changes in biomolecular interactions is provided. The application of HP-SPR was extended to the use of commercially available sensor chips. We have shown that BIAcore(TM) SA chips maintain their surface binding functionality after pressure exposure and that effects to the surface are reversible to 6000 psi. Three test systems were chosen to be studied using this instrument, each having different characteristics; cytochrome c association to cytochrome b5, unfolding of staphylococcal nuclease, and binding of the BamH1 restriction enzyme to its DNA recognition site.","Made available in DSpace on 2015-09-25T22:13:13Z (GMT). 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