{"id":{"repo_id":"utswmed","oai_identifier":"oai:utswmed-ir.tdl.org:2152.5/275"},"canonical_url":"https://search.dev.ndltd.org/etd/utswmed/oai:utswmed-ir.tdl.org:2152.5/275","repository":{"repo_id":"utswmed","name":"University of Texas Southwestern Medical Center","base_url":"https://utswmed-ir.tdl.org/server/oai/request"},"display":{"title":"Detection of Polypeptide Interactions Via Periodate Triggered Dopa Crosslinking","abstract":"Protein-Protein interactions mediate most biological function, yet elucidation of the molecular architecture within a cell still remains a formidable challenge for molecular biologist. We have developed a novel, bioorthogonal cross-linking chemistry based upon periodate mediated oxidation of the artificial amino acid 3,4- Dihydroxyphenylalanine to a resultant ortho-quinone. This ortho-quinone was proven capable of capturing either cysteine, lysine, histidine, or a peptidyl alpha -amine in templated chemical reactions. After elucidating the chemistry, we describe utilization of this methodology to map peptide-protein interactions between the 26S proteasome and activation domains as well as the Arp 2/3 complex and the CA peptide. Finally, we present the creation of a chimeric molecule consisting of the biarsencial fluorescent reporter FLAsH conjugated to 3,4-Dihydroxyphenylalanine as a route to deliver 3,4-dihydroxyphenylalanine site specifically to a protein of interest and probe for protein-protein interactions partners in cell lysates.","abstract_html":"Protein-Protein interactions mediate most biological function, yet elucidation of the molecular architecture within a cell still remains a formidable challenge for molecular biologist. We have developed a novel, bioorthogonal cross-linking chemistry based upon periodate mediated oxidation of the artificial amino acid 3,4- Dihydroxyphenylalanine to a resultant ortho-quinone. This ortho-quinone was proven capable of capturing either cysteine, lysine, histidine, or a peptidyl alpha -amine in templated chemical reactions. After elucidating the chemistry, we describe utilization of this methodology to map peptide-protein interactions between the 26S proteasome and activation domains as well as the Arp 2/3 complex and the CA peptide. Finally, we present the creation of a chimeric molecule consisting of the biarsencial fluorescent reporter FLAsH conjugated to 3,4-Dihydroxyphenylalanine as a route to deliver 3,4-dihydroxyphenylalanine site specifically to a protein of interest and probe for protein-protein interactions partners in cell lysates.","abstract_has_math":false,"creators":["Burdine, Lyle Jackson"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Kodadek, Thomas J."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2010,"date_issued":"2010-07-12T17:24:15Z","date_published":"2010-07-12T17:24:15Z","updated_at":"2026-07-24T05:52:24Z","subjects":["Protein Interaction Mapping","Intracellular Signaling Peptides and Proteins","Dihydroxyphenylalanine"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["71150591"],"render_values":[{"text":"71150591","href":null,"code":true}]}]},"links":{"outbound_url":"https://hdl.handle.net/2152.5/275","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Kodadek, Thomas J."]},{"key":"dc:creator","label":"Author","values":["Burdine, Lyle Jackson"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2010-07-12T17:24:15Z","2006-08-11"]},{"key":"dc:type","label":"Dc Type","values":["Thesis","Text","dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Protein Interaction Mapping","Intracellular Signaling Peptides and Proteins","Dihydroxyphenylalanine"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://hdl.handle.net/2152.5/275","71150591"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Protein-Protein interactions mediate most biological function, yet elucidation of the molecular architecture within a cell still remains a formidable challenge for molecular biologist. We have developed a novel, bioorthogonal cross-linking chemistry based upon periodate mediated oxidation of the artificial amino acid 3,4- Dihydroxyphenylalanine to a resultant ortho-quinone. This ortho-quinone was proven capable of capturing either cysteine, lysine, histidine, or a peptidyl alpha -amine in templated chemical reactions. After elucidating the chemistry, we describe utilization of this methodology to map peptide-protein interactions between the 26S proteasome and activation domains as well as the Arp 2/3 complex and the CA peptide. Finally, we present the creation of a chimeric molecule consisting of the biarsencial fluorescent reporter FLAsH conjugated to 3,4-Dihydroxyphenylalanine as a route to deliver 3,4-dihydroxyphenylalanine site specifically to a protein of interest and probe for protein-protein interactions partners in cell lysates."]},{"key":"dc:format","label":"Dc Format","values":["Electronic","application/pdf","born digital"]},{"key":"dc:title","label":"Title","values":["Detection of Polypeptide Interactions Via Periodate Triggered Dopa Crosslinking"]}]}],"canonical_facts":{"dc:contributor":["Kodadek, Thomas J."],"dc:creator":["Burdine, Lyle Jackson"],"dc:date":["2010-07-12T17:24:15Z","2006-08-11"],"dc:description":["Protein-Protein interactions mediate most biological function, yet elucidation of the molecular architecture within a cell still remains a formidable challenge for molecular biologist. We have developed a novel, bioorthogonal cross-linking chemistry based upon periodate mediated oxidation of the artificial amino acid 3,4- Dihydroxyphenylalanine to a resultant ortho-quinone. This ortho-quinone was proven capable of capturing either cysteine, lysine, histidine, or a peptidyl alpha -amine in templated chemical reactions. After elucidating the chemistry, we describe utilization of this methodology to map peptide-protein interactions between the 26S proteasome and activation domains as well as the Arp 2/3 complex and the CA peptide. Finally, we present the creation of a chimeric molecule consisting of the biarsencial fluorescent reporter FLAsH conjugated to 3,4-Dihydroxyphenylalanine as a route to deliver 3,4-dihydroxyphenylalanine site specifically to a protein of interest and probe for protein-protein interactions partners in cell lysates."],"dc:format":["Electronic","application/pdf","born digital"],"dc:identifier":["https://hdl.handle.net/2152.5/275","71150591"],"dc:language":["en"],"dc:subject":["Protein Interaction Mapping","Intracellular Signaling Peptides and Proteins","Dihydroxyphenylalanine"],"dc:title":["Detection of Polypeptide Interactions Via Periodate Triggered Dopa Crosslinking"],"dc:type":["Thesis","Text","dissertation"]},"updated_at":"2026-07-24T05:52:24Z"}