Use of solution-state nuclear magnetic resonance spectroscopy to determine the structures of medicinally relevant peptides and proteins

Shea, Lindsey

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https://hdl.handle.net/2142/34455 Copy

Description

Title

Use of solution-state nuclear magnetic resonance spectroscopy to determine the structures of medicinally relevant peptides and proteins

Author(s)

Shea, Lindsey

Issue Date

2012-09-18T21:18:02Z

Director of Research (if dissertation) or Advisor (if thesis)

van der Donk, Wilfred A.

Department of Study

Chemistry

Discipline

Chemistry

Degree Granting Institution

University of Illinois at Urbana-Champaign

Degree Name

M.S.

Degree Level

Thesis

Keyword(s)

• nuclear magnetic resonance (NMR)spectroscopy
• Lantibiotics
• Lantipeptides
• immunity
• phosphite dehydrogenase
• prochlorosin
• cytolysin
• NisI

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.

Graduation Semester

2012-08

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http://hdl.handle.net/2142/34455

Copyright and License Information

Copyright 2012 Lindsey Shea

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