ingest cdrApp 2017-07-06T11:48:18.446Z 082b3de9-6030-4a3e-a983-035a47fc699e modifyDatastreamByValue RELS-EXT fedoraAdmin 2017-07-06T11:52:50.198Z Setting exclusive relation modifyDatastreamByValue RELS-EXT fedoraAdmin 2017-07-06T11:52:51.309Z Setting exclusive relation addDatastream MD_TECHNICAL fedoraAdmin 2017-07-06T11:52:59.392Z Adding technical metadata derived by FITS modifyDatastreamByValue RELS-EXT fedoraAdmin 2017-07-06T11:53:00.056Z Setting exclusive relation addDatastream MD_FULL_TEXT fedoraAdmin 2017-07-06T11:53:01.339Z Adding full text metadata extracted by Apache Tika modifyDatastreamByValue RELS-EXT fedoraAdmin 2017-07-06T11:53:18.415Z Setting exclusive relation modifyDatastreamByValue RELS-EXT cdrApp 2017-07-06T12:26:43.183Z Setting exclusive relation modifyDatastreamByValue MD_DESCRIPTIVE cdrApp 2018-01-04T18:03:48.779Z modifyDatastreamByValue MD_DESCRIPTIVE cdrApp 2018-01-25T12:43:08.018Z modifyDatastreamByValue MD_DESCRIPTIVE cdrApp 2018-01-27T12:43:07.853Z modifyDatastreamByValue MD_DESCRIPTIVE cdrApp 2018-03-14T09:48:49.957Z modifyDatastreamByValue MD_DESCRIPTIVE cdrApp 2018-05-17T21:24:38.016Z modifyDatastreamByValue MD_DESCRIPTIVE cdrApp 2018-07-11T08:18:20.115Z modifyDatastreamByValue MD_DESCRIPTIVE cdrApp 2018-07-18T04:27:30.252Z modifyDatastreamByValue MD_DESCRIPTIVE cdrApp 2018-08-16T17:34:39.697Z modifyDatastreamByValue MD_DESCRIPTIVE cdrApp 2018-09-27T13:19:00.621Z modifyDatastreamByValue MD_DESCRIPTIVE cdrApp 2018-10-12T04:33:55.714Z modifyDatastreamByValue MD_DESCRIPTIVE cdrApp 2019-03-21T14:16:20.122Z Gregry Woss Author Department of Chemistry College of Arts and Sciences DEVELOPMENT OF A PEPTIDE BASED E3 LIGASE REPORTER This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. Spring 2017 2017 Analytical chemistry Capillary Electrophoresis, E3 Ligase, Peptide, Peptide Reporters eng Doctor of Philosophy Dissertation University of North Carolina at Chapel Hill Graduate School Degree granting institution Chemistry Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor Mark Wightman Thesis advisor Marcey Waters Thesis advisor Mathew Lockett Thesis advisor text Gregery Woss Author Department of Chemistry College of Arts and Sciences Development of Peptide Based E3 Ligase Reporter This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. Spring 2017 2017 Analytical chemistry Capillary Electrophoresis, E3 Ligase, Peptide, Peptide Reporters eng Doctor of Philosophy Dissertation University of North Carolina at Chapel Hill Graduate School Degree granting institution Chemistry Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor Mark Wightman Thesis advisor Marcey Waters Thesis advisor Mathew Lockett Thesis advisor text Gregery Woss Creator Department of Chemistry College of Arts and Sciences Development of Peptide Based E3 Ligase Reporter This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. Spring 2017 2017 Analytical chemistry Capillary Electrophoresis, E3 Ligase, Peptide, Peptide Reporters eng Doctor of Philosophy Dissertation University of North Carolina at Chapel Hill Graduate School Degree granting institution Chemistry Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor Mark Wightman Thesis advisor Marcey Waters Thesis advisor Mathew Lockett Thesis advisor text Gregery Woss Creator Department of Chemistry College of Arts and Sciences Development of Peptide Based E3 Ligase Reporter This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. Spring 2017 2017 Analytical chemistry Capillary Electrophoresis, E3 Ligase, Peptide, Peptide Reporters eng Doctor of Philosophy Dissertation University of North Carolina at Chapel Hill Graduate School Degree granting institution Chemistry Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor Mark Wightman Thesis advisor Marcey Waters Thesis advisor Mathew Lockett Thesis advisor text Gregery Woss Creator Department of Chemistry College of Arts and Sciences Development of Peptide Based E3 Ligase Reporter This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. 2017-05 2017 Analytical chemistry Capillary Electrophoresis, E3 Ligase, Peptide, Peptide Reporters eng Doctor of Philosophy Dissertation University of North Carolina at Chapel Hill Graduate School Degree granting institution Chemistry Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor Mark Wightman Thesis advisor Marcey Waters Thesis advisor Mathew Lockett Thesis advisor text Gregery Woss Creator Department of Chemistry College of Arts and Sciences Development of Peptide Based E3 Ligase Reporter This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. 2017 Analytical chemistry Capillary Electrophoresis, E3 Ligase, Peptide, Peptide Reporters eng Doctor of Philosophy Dissertation University of North Carolina at Chapel Hill Graduate School Degree granting institution Chemistry Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor Mark Wightman Thesis advisor Marcey Waters Thesis advisor Mathew Lockett Thesis advisor text 2017-05 Gregery Woss Creator Department of Chemistry College of Arts and Sciences Development of Peptide Based E3 Ligase Reporter This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. 2017 Analytical chemistry Capillary Electrophoresis, E3 Ligase, Peptide, Peptide Reporters eng Doctor of Philosophy Dissertation University of North Carolina at Chapel Hill Graduate School Degree granting institution Chemistry Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor Mark Wightman Thesis advisor Marcey Waters Thesis advisor Mathew Lockett Thesis advisor text 2017-05 Gregery Woss Creator Department of Chemistry College of Arts and Sciences Development of Peptide Based E3 Ligase Reporter This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. 2017 Analytical chemistry Capillary Electrophoresis, E3 Ligase, Peptide, Peptide Reporters eng Doctor of Philosophy Dissertation University of North Carolina at Chapel Hill Graduate School Degree granting institution Chemistry Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor Mark Wightman Thesis advisor Marcey Waters Thesis advisor Mathew Lockett Thesis advisor text 2017-05 Gregery Woss Creator Department of Chemistry College of Arts and Sciences Development of Peptide Based E3 Ligase Reporter This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. 2017 Analytical chemistry Capillary Electrophoresis, E3 Ligase, Peptide, Peptide Reporters eng Doctor of Philosophy Dissertation Chemistry Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor R. Mark Wightman Thesis advisor Marcey Waters Thesis advisor Matthew Lockett Thesis advisor text 2017-05 University of North Carolina at Chapel Hill Degree granting institution Gregery Woss Creator Department of Chemistry College of Arts and Sciences Development of Peptide Based E3 Ligase Reporter This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. 2017 Analytical chemistry Capillary Electrophoresis; E3 Ligase; Peptide; Peptide Reporters eng Doctor of Philosophy Dissertation Chemistry Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor R. Mark Wightman Thesis advisor Marcey Waters Thesis advisor Matthew Lockett Thesis advisor text 2017-05 University of North Carolina at Chapel Hill Degree granting institution Gregery Woss Creator Department of Chemistry College of Arts and Sciences Development of Peptide Based E3 Ligase Reporter This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. 2017 Analytical chemistry Capillary Electrophoresis, E3 Ligase, Peptide, Peptide Reporters eng Doctor of Philosophy Dissertation University of North Carolina at Chapel Hill Graduate School Degree granting institution Chemistry Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor R. Mark Wightman Thesis advisor Marcey Waters Thesis advisor Matthew Lockett Thesis advisor text 2017-05 Gregery Woss Creator Department of Chemistry College of Arts and Sciences This dissertation describes the development of a new analytical tool capable of analyzing E3 ligase activity, a critical element in the ubiquitin proteasome system. This was accomplished through the development of a novel class of peptide-based fluorescent E3 ligase reporters which are intended to be analyzed by capillary electrophoresis (CE). These E3 ligase reporters incorporate a degradation signal, or degron, which is recognized and ubiquitinated by an E3 ligase, as well as a fluorescent tag to facilitate detection by laser induced fluorescence (LIF). In order to identify potent degrons, a library of E3 ligase reporters incorporating degrons from various sources was synthesized. These reporters were characterized in cell lysates, then optimized to produce substrates that would be efficiently ubiquitinated in cells. In addition to working with minimal degron sequences, an expanded sub-library of reporters based around the degron isolated from p53 was characterized in order to identify a compact degron element and investigate its ubiquitination kinetics and specificity. In order to circumvent peptidase-mediated degradation, a traditional weakness of peptide reporters, investigations were also carried out to develop novel degradation-resistant E3 ligase reporters incorporating β-hairpin secondary structures. Serendipitously, a β-hairpin that was both peptidase-resistant and functioned as an E3 ligase reporter was identified. Finally, electrophoretic separation conditions for the analysis of E3 ligase peptide reporters were identified, and ubiquitination of E3 ligase reporters in cell lysates was observed by CE-LIF. This dissertation lays the groundwork for future development of next generation peptide-based E3 ligase reporters. 2017 Analytical chemistry Capillary Electrophoresis; E3 Ligase; Peptide; Peptide Reporters eng Doctor of Philosophy Dissertation University of North Carolina at Chapel Hill Graduate School Degree granting institution Nancy Allbritton Thesis advisor James Jorgenson Thesis advisor R. Mark Wightman Thesis advisor Marcey Waters Thesis advisor Matthew Lockett Thesis advisor text 2017-05 Woss_unc_0153D_16875.pdf uuid:3768a2c6-60aa-4a9e-8ed3-3f39a0301919 proquest 2017-04-12T15:50:52Z 2019-07-06T00:00:00 application/pdf 3886014 yes