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.
","abstract_html":"<p>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.</p>","abstract_has_math":false,"creators":["Callahan, Courtney Tenille"],"institution":null,"degree_name":"Ph.D.","degree_level":"Campus Access Dissertation","degree_discipline":"Biomedical Science","degree_department":null,"school":null,"contributors":["Richard Hunt"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2012,"date_issued":"2012-01-01T08:00:00Z","date_published":"2012-01-01T08:00:00Z","updated_at":"2026-07-24T04:38:37Z","subjects":["Biomedical","Chemicals and Drugs","Medicine and Health Sciences","bacteria","bacteriophage","MALDI MS","proteins","proteomics","SDS-PAGE"],"languages":[],"rights":["© 2012, Courtney Tenille Callahan"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://scholarcommons.sc.edu/etd/2093","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Richard Hunt"]},{"key":"dc:creator","label":"Author","values":["Callahan, Courtney Tenille"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_discipline","label":"Discipline","values":["Biomedical Science"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Campus Access Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biomedical","Chemicals and Drugs","Medicine and Health Sciences","bacteria","bacteriophage","MALDI MS","proteins","proteomics","SDS-PAGE"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["© 2012, Courtney Tenille Callahan"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://scholarcommons.sc.edu/etd/2093"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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.
"]},{"key":"dc:title","label":"Title","values":["Identification and Characterization of Bacterial and Bacteriophage Proteins Via Matrix-Assisted Laser Desorption Ionization (Maldi) Mass Spectrometry"]}]}],"canonical_facts":{"dc:contributor":["Richard Hunt"],"dc:creator":["Callahan, Courtney Tenille"],"dc:description.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.
"],"dc:identifier":["https://scholarcommons.sc.edu/etd/2093"],"dc:rights":["© 2012, Courtney Tenille Callahan"],"dc:subject":["Biomedical","Chemicals and Drugs","Medicine and Health Sciences","bacteria","bacteriophage","MALDI MS","proteins","proteomics","SDS-PAGE"],"dc:title":["Identification and Characterization of Bacterial and Bacteriophage Proteins Via Matrix-Assisted Laser Desorption Ionization (Maldi) Mass Spectrometry"],"thesis:degree_discipline":["Biomedical Science"],"thesis:degree_level":["Campus Access Dissertation"],"thesis:degree_name":["Ph.D."]},"updated_at":"2026-07-24T04:38:37Z"}