2026-09-21T17:13:34Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/34455 2023-07-11 col_2142_5131 col_2142_14789 com_2142_5130 com_2142_14788 com_2142_8903

van der Donk, Wilfred A. Shea, Lindsey 2012-09-18T21:18:02Z 2012-09-18T21:18:02Z 2014-09-18T10:00:41Z 2012-08 2012-09-18T21:18:02Z 2012-08 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 Item withdrawn by Mark Zulauf (zulauf@illinois.edu) on 2012-07-17T17:41:28Z Item was in collections: University of Illinois Theses & Dissertations (ID: 1) No. of bitstreams: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. http://hdl.handle.net/2142/34455 en Copyright 2012 Lindsey Shea nuclear magnetic resonance (NMR)spectroscopy Lantibiotics Lantipeptides immunity phosphite dehydrogenase prochlorosin cytolysin NisI Use of solution-state nuclear magnetic resonance spectroscopy to determine the structures of medicinally relevant peptides and proteins Chemistry 1413 Chemistry 0335 University of Illinois at Urbana-Champaign Thesis M.S. MS:Chemistry -UIUC 10KS0335MS