{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/34455"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/34455","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Use of solution-state nuclear magnetic resonance spectroscopy to determine the structures of medicinally relevant peptides and proteins","abstract":"The research described herein details various studies with solution-state nuclear magnetic resonance (NMR) spectroscopy to aid in the elucidation of structures of various medicinally relevant peptides. The first system studied was that of the prochlorosins, an unusual family of lantipeptides all modified to their mature form by a single lantibiotic synthetase. Next was the two peptide lantibiotic cytolysin, unique among bacteriocins in that it has hemolytic activity in addition to bactericidal activity. Nisin, the prototypical lantibiotic, was studied in the context of the immunity protein, NisI, which is believed to confer immunity against lysis to the producing organism. The final system was phosphite dehydrogenase, an enzyme putatively useful in the regeneration of nicotinamide cofactors. By studying these systems, it is believed that advances could be made toward novel antibiotic compounds to alleviate the increasing pressure of resistance seen in clinical settings.","abstract_html":"The research described herein details various studies with solution-state nuclear magnetic resonance (NMR) spectroscopy to aid in the elucidation of structures of various medicinally relevant peptides. The first system studied was that of the prochlorosins, an unusual family of lantipeptides all modified to their mature form by a single lantibiotic synthetase. Next was the two peptide lantibiotic cytolysin, unique among bacteriocins in that it has hemolytic activity in addition to bactericidal activity. Nisin, the prototypical lantibiotic, was studied in the context of the immunity protein, NisI, which is believed to confer immunity against lysis to the producing organism. The final system was phosphite dehydrogenase, an enzyme putatively useful in the regeneration of nicotinamide cofactors. By studying these systems, it is believed that advances could be made toward novel antibiotic compounds to alleviate the increasing pressure of resistance seen in clinical settings.","abstract_has_math":false,"creators":["Shea, Lindsey"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"M.S.","degree_level":"Thesis","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["van der Donk, Wilfred A."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2012,"date_issued":"2012-09-18T21:18:02Z","date_published":"2012-09-18T21:18:02Z","updated_at":"2026-07-22T22:25:31Z","subjects":["nuclear magnetic resonance (NMR)spectroscopy","Lantibiotics","Lantipeptides","immunity","phosphite dehydrogenase","prochlorosin","cytolysin","NisI"],"languages":["en"],"rights":["Copyright 2012 Lindsey Shea"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/2142/34455","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["van der Donk, Wilfred A."]},{"key":"dc:creator","label":"Author","values":["Shea, Lindsey"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2012-09-18T21:18:02Z","2014-09-18T10:00:41Z","2012-08"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["M.S."]},{"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":["nuclear magnetic resonance (NMR)spectroscopy","Lantibiotics","Lantipeptides","immunity","phosphite dehydrogenase","prochlorosin","cytolysin","NisI"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 2012 Lindsey Shea"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/34455"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The research described herein details various studies with solution-state nuclear magnetic resonance (NMR) spectroscopy to aid in the elucidation of structures of various medicinally relevant peptides. The first system studied was that of the prochlorosins, an unusual family of lantipeptides all modified to their mature form by a single lantibiotic synthetase. Next was the two peptide lantibiotic cytolysin, unique among bacteriocins in that it has hemolytic activity in addition to bactericidal activity. Nisin, the prototypical lantibiotic, was studied in the context of the immunity protein, NisI, which is believed to confer immunity against lysis to the producing organism. The final system was phosphite dehydrogenase, an enzyme putatively useful in the regeneration of nicotinamide cofactors. By studying these systems, it is believed that advances could be made toward novel antibiotic compounds to alleviate the increasing pressure of resistance seen in clinical settings.","Item withdrawn by Mark Zulauf (zulauf@illinois.edu) on 2012-07-17T17:41:28Z Item was in collections: University of Illinois Theses & Dissertations (ID: 1) No. of bitstreams: 1 SHEA_LINDSEY.pdf: 32581215 bytes, checksum: 2e3b86dbefd9f1405f42cb11207a75b3 (MD5)","Made available in DSpace on 2012-09-18T21:18:02Z (GMT). No. of bitstreams: 2 shea_lindsey.pdf: 32581520 bytes, checksum: 5f55378870751948bb34508512cfe5f0 (MD5) license.txt: 4062 bytes, checksum: 457a2f4bd68654e3cb029a8a0b263302 (MD5)","Restriction data tranferred 2014-07-01T11:11:32-05:00 Original Data Group with Access UIUC Users [automated] Release Date: 2014-09-18 16:21:01 UTC Reason: Author requested U of Illinois access only (OA after 2yrs) in Vireo ETD system","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Seth Robbins (srobbins@illinois.edu) on 2012-09-18T21:21:07Z Item is restricted until 2014-09-18T21:21:01Z","U of I Only Restriction Lifted for Item 34729 on 2014-09-18T10:00:41Z."]},{"key":"dc:title","label":"Title","values":["Use of solution-state nuclear magnetic resonance spectroscopy to determine the structures of medicinally relevant peptides and proteins"]}]}],"canonical_facts":{"dc:contributor":["van der Donk, Wilfred A."],"dc:creator":["Shea, Lindsey"],"dc:date":["2012-09-18T21:18:02Z","2014-09-18T10:00:41Z","2012-08"],"dc:description":["The research described herein details various studies with solution-state nuclear magnetic resonance (NMR) spectroscopy to aid in the elucidation of structures of various medicinally relevant peptides. The first system studied was that of the prochlorosins, an unusual family of lantipeptides all modified to their mature form by a single lantibiotic synthetase. Next was the two peptide lantibiotic cytolysin, unique among bacteriocins in that it has hemolytic activity in addition to bactericidal activity. Nisin, the prototypical lantibiotic, was studied in the context of the immunity protein, NisI, which is believed to confer immunity against lysis to the producing organism. The final system was phosphite dehydrogenase, an enzyme putatively useful in the regeneration of nicotinamide cofactors. By studying these systems, it is believed that advances could be made toward novel antibiotic compounds to alleviate the increasing pressure of resistance seen in clinical settings.","Item withdrawn by Mark Zulauf (zulauf@illinois.edu) on 2012-07-17T17:41:28Z Item was in collections: University of Illinois Theses & Dissertations (ID: 1) No. of bitstreams: 1 SHEA_LINDSEY.pdf: 32581215 bytes, checksum: 2e3b86dbefd9f1405f42cb11207a75b3 (MD5)","Made available in DSpace on 2012-09-18T21:18:02Z (GMT). No. of bitstreams: 2 shea_lindsey.pdf: 32581520 bytes, checksum: 5f55378870751948bb34508512cfe5f0 (MD5) license.txt: 4062 bytes, checksum: 457a2f4bd68654e3cb029a8a0b263302 (MD5)","Restriction data tranferred 2014-07-01T11:11:32-05:00 Original Data Group with Access UIUC Users [automated] Release Date: 2014-09-18 16:21:01 UTC Reason: Author requested U of Illinois access only (OA after 2yrs) in Vireo ETD system","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Seth Robbins (srobbins@illinois.edu) on 2012-09-18T21:21:07Z Item is restricted until 2014-09-18T21:21:01Z","U of I Only Restriction Lifted for Item 34729 on 2014-09-18T10:00:41Z."],"dc:identifier":["http://hdl.handle.net/2142/34455"],"dc:language":["en"],"dc:rights":["Copyright 2012 Lindsey Shea"],"dc:subject":["nuclear magnetic resonance (NMR)spectroscopy","Lantibiotics","Lantipeptides","immunity","phosphite dehydrogenase","prochlorosin","cytolysin","NisI"],"dc:title":["Use of solution-state nuclear magnetic resonance spectroscopy to determine the structures of medicinally relevant peptides and proteins"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["M.S."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:31Z"}