Date of Award

1-1-2012

Document Type

Campus Access Dissertation

Department

Biomedical Science

First Advisor

Richard Hunt

Abstract

The identification, characterization and quantification of all proteins involved in a particular pathway, organelle, cell, tissue, organ or organism that can be studied in concert to provide accurate and comprehensive data about that system is called proteomics. Proteomics is formalized by combining the techniques for large-scale separation (SDS-PAGE) with very precise, high fidelity approaches to the analysis and characterization of the separated proteins (mass spectrometry). Protein analysis is an underutilized tool that can serve as a valuable alternative to DNA for the identification and characterization of microorganisms. Driven by the need to identify, characterize, and quantify proteins at ever increasing sensitivity and in ever more complex samples, a wide range of mass spectrometry-based analytical platforms and experimental strategies have emerged. Here, it is shown how using matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry, coupled with sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), one can identify and characterize bacterial and bacteriophage proteins.

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