{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84305"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84305","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Development and Application of Next Generation Mass Spectrometry for Protein Analysis at High-Resolution","abstract":"And finally, a high-resolution MS/MS platform was developed to analyze large peptides at >>50,000 resolving power along with a software suite for interpreting resolved isotopic distributions and handling all known protein modifications on a high throughput basis. Called Middle Down Proteomics, this process identified 7454 peptides from 2-20 kDa (1472 unique) from 555 proteins after just 23 LC-MS/MS injections. Along with greatly increased confidence for peptide identification (expectation values from 10-89 to 104) and characterization (up to 20% of peptides were detected as modified in some LC-MS/MS runs), fragmentation data with <2 ppm accuracy also enabled error tolerant and multiplexed database searching---all clearly demonstrated in this thesis.","abstract_html":"And finally, a high-resolution MS/MS platform was developed to analyze large peptides at &gt;&gt;50,000 resolving power along with a software suite for interpreting resolved isotopic distributions and handling all known protein modifications on a high throughput basis. Called Middle Down Proteomics, this process identified 7454 peptides from 2-20 kDa (1472 unique) from 555 proteins after just 23 LC-MS/MS injections. Along with greatly increased confidence for peptide identification (expectation values from 10-89 to 104) and characterization (up to 20% of peptides were detected as modified in some LC-MS/MS runs), fragmentation data with &lt;2 ppm accuracy also enabled error tolerant and multiplexed database searching---all clearly demonstrated in this thesis.","abstract_has_math":false,"creators":["Boyne, Michael Thomas, II"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Kelleher, Neil L."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:13:53Z","date_published":"2015-09-25T22:13:53Z","updated_at":"2026-07-22T22:26:23Z","subjects":["Chemistry, Analytical"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3337728"],"render_values":[{"text":"(MiAaPQ)AAI3337728","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84305","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Kelleher, Neil L."]},{"key":"dc:creator","label":"Author","values":["Boyne, Michael Thomas, II"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:13:53Z","10000-01-01","2008"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"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":["Chemistry, Analytical"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/84305","(MiAaPQ)AAI3337728"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["And finally, a high-resolution MS/MS platform was developed to analyze large peptides at >>50,000 resolving power along with a software suite for interpreting resolved isotopic distributions and handling all known protein modifications on a high throughput basis. 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