{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/78610"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/78610","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Kinetics and thermodynamics of protein-RNA interactions and protein folding in vitro and in cells","abstract":"This Dissertation was approved for publication on 2015-04-20 at 07:49.","abstract_html":"This Dissertation was approved for publication on 2015-04-20 at 07:49.","abstract_has_math":false,"creators":["Guzman Sanchez, Irisbel"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Gruebele, Martin","Martin Gruebele","Gennis, Robert","Ha, Taekjip","Ceman, Stephanie S."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-07-22T22:33:17Z","date_published":"2015-07-22T22:33:17Z","updated_at":"2026-07-22T22:26:12Z","subjects":["Protein-RNA interactions","protein folding","fluorescence","fluorescence resonance energy transfer (FRET)","fast relaxation imagining (FREI)","temperature jump"],"languages":["en"],"rights":["2015 Irisbel Guzman Sanchez"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/2142/78610","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Gruebele, Martin","Martin Gruebele","Gennis, Robert","Ha, Taekjip","Ceman, Stephanie S."]},{"key":"dc:creator","label":"Author","values":["Guzman Sanchez, Irisbel"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-07-22T22:33:17Z","2017-07-23T09:15:30Z","2015-05","2015-04-20","2015-5"]},{"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":["Protein-RNA interactions","protein folding","fluorescence","fluorescence resonance energy transfer (FRET)","fast relaxation imagining (FREI)","temperature jump"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["2015 Irisbel Guzman Sanchez"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/78610"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["This Dissertation was approved for publication on 2015-04-20 at 07:49.","DSpace SAF Submission Ingestion Package generated from Vireo submission #7831 on 2015-07-22 at 14:17:43","Made available in DSpace on 2015-07-22T22:33:17Z (GMT). No. of bitstreams: 2 GUZMANSANCHEZ-DISSERTATION-2015.pdf: 62642409 bytes, checksum: 317b448aff4617eee2415df8b1ec6c15 (MD5) LICENSE.txt: 4219 bytes, checksum: 1033337e83f09b92467dfd58346a8f9b (MD5) Previous issue date: 2015-04-20","Embargo set by: Seth Robbins for item 79851 Lift date: 2017-07-22T22:34:16Z Reason: Author requested U of Illinois access only (OA after 2yrs) in Vireo ETD system","Protein-RNA interactions and protein folding are critical subjects in biochemistry, because of their significance during the formation of active complexes and signaling pathways. Regardless of the substantial amount of studies in the fields of protein-RNA interactions and protein folding, little is known about the stability and kinetics of these in the cell. This doctoral dissertation aims to advance the understanding of protein-RNA interactions and protein folding inside cells through comparative in vitro studies, utilizing U1A-SL2 RNA complex and PGK/VlsE proteins as model systems, respectively. For the protein-RNA studies, dynamics experiments of one positive charged mutant of the spliceosomal U1A protein, the golden model for the RNA Recognition Motif (RRM), reveled a conformational transition for the protein only. Also, U1A-SL2 RNA dissociation kinetics studies with U1A positive charged mutants supported the previously proposed two-step dissociation pathway and demonstrated the importance of positive charge residues. The U1A-SL2 was also investigated in macromolecular crowded buffers were its binding affinity increased. It was also studied inside mammalian cells were it localized in the nucleus and its binding affinity decreased. For the protein folding studies, the extracellular VlsE antigen was found to be destabilized inside mammalian cells opposed to the intracellular PGK enzyme.","Submission published under a 24 month embargo labeled 'U of I only', the embargo will last until 2017-05-01","The student, Irisbel Guzman Sanchez, accepted the attached license on 2015-04-12 at 22:18.","The student, Irisbel Guzman Sanchez, submitted this Dissertation for approval on 2015-04-12 at 22:33.","U of I Only Restriction Lifted for Item 79851 on 2017-07-23T09:15:30Z."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Kinetics and thermodynamics of protein-RNA interactions and protein folding in vitro and in cells"]}]}],"canonical_facts":{"dc:contributor":["Gruebele, Martin","Martin Gruebele","Gennis, Robert","Ha, Taekjip","Ceman, Stephanie S."],"dc:creator":["Guzman Sanchez, Irisbel"],"dc:date":["2015-07-22T22:33:17Z","2017-07-23T09:15:30Z","2015-05","2015-04-20","2015-5"],"dc:description":["This Dissertation was approved for publication on 2015-04-20 at 07:49.","DSpace SAF Submission Ingestion Package generated from Vireo submission #7831 on 2015-07-22 at 14:17:43","Made available in DSpace on 2015-07-22T22:33:17Z (GMT). No. of bitstreams: 2 GUZMANSANCHEZ-DISSERTATION-2015.pdf: 62642409 bytes, checksum: 317b448aff4617eee2415df8b1ec6c15 (MD5) LICENSE.txt: 4219 bytes, checksum: 1033337e83f09b92467dfd58346a8f9b (MD5) Previous issue date: 2015-04-20","Embargo set by: Seth Robbins for item 79851 Lift date: 2017-07-22T22:34:16Z Reason: Author requested U of Illinois access only (OA after 2yrs) in Vireo ETD system","Protein-RNA interactions and protein folding are critical subjects in biochemistry, because of their significance during the formation of active complexes and signaling pathways. Regardless of the substantial amount of studies in the fields of protein-RNA interactions and protein folding, little is known about the stability and kinetics of these in the cell. This doctoral dissertation aims to advance the understanding of protein-RNA interactions and protein folding inside cells through comparative in vitro studies, utilizing U1A-SL2 RNA complex and PGK/VlsE proteins as model systems, respectively. For the protein-RNA studies, dynamics experiments of one positive charged mutant of the spliceosomal U1A protein, the golden model for the RNA Recognition Motif (RRM), reveled a conformational transition for the protein only. Also, U1A-SL2 RNA dissociation kinetics studies with U1A positive charged mutants supported the previously proposed two-step dissociation pathway and demonstrated the importance of positive charge residues. The U1A-SL2 was also investigated in macromolecular crowded buffers were its binding affinity increased. It was also studied inside mammalian cells were it localized in the nucleus and its binding affinity decreased. For the protein folding studies, the extracellular VlsE antigen was found to be destabilized inside mammalian cells opposed to the intracellular PGK enzyme.","Submission published under a 24 month embargo labeled 'U of I only', the embargo will last until 2017-05-01","The student, Irisbel Guzman Sanchez, accepted the attached license on 2015-04-12 at 22:18.","The student, Irisbel Guzman Sanchez, submitted this Dissertation for approval on 2015-04-12 at 22:33.","U of I Only Restriction Lifted for Item 79851 on 2017-07-23T09:15:30Z."],"dc:format":["application/pdf"],"dc:identifier":["http://hdl.handle.net/2142/78610"],"dc:language":["en"],"dc:rights":["2015 Irisbel Guzman Sanchez"],"dc:subject":["Protein-RNA interactions","protein folding","fluorescence","fluorescence resonance energy transfer (FRET)","fast relaxation imagining (FREI)","temperature jump"],"dc:title":["Kinetics and thermodynamics of protein-RNA interactions and protein folding in vitro and in cells"],"dc:type":["text"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:12Z"}