{"id":{"repo_id":"ecu","oai_identifier":"oai:thescholarship.ecu.edu:10342/7434"},"canonical_url":"https://search.dev.ndltd.org/etd/ecu/oai:thescholarship.ecu.edu:10342/7434","repository":{"repo_id":"ecu","name":"East Carolina University","base_url":"https://thescholarship.ecu.edu/server/oai/request"},"display":{"title":"Studying Collagen with PyrATS: Pyrene-Appended Trimeric Systems","abstract":"Collagens are a family of triple-helical structural proteins that are ubiquitous in vertebrates. Improper folding of collagen can lead to disorders such as osteogenesis imperfecta, or \"brittle bone disease.\" There is significant interest in understanding the factors that drive collagen folding and stability, but studying native collagens is difficult because they are hundreds of amino acids in length. This thesis describes a series of well-characterized (Pro-Hyp-Gly)7 model peptides which have been tagged at their N-termini with the fluorophore pyrene. When in close contact, pyrene units can form excimers that emit low-energy light. This allows for the study of several fundamental questions in collagen research using fluorescence spectroscopy, including concentration dependence, folding directionality, and local fraying, upon solutions that are significantly more dilute than those customarily used in circular dichroism (CD) experiments. Notably, for most of the peptides studied, there is agreement between the melting temperatures (Tm) obtained via fluorescence and CD techniques. In addition, the pyrene probes were found to provide a situational increase in thermal stability of triple helices.","abstract_html":"Collagens are a family of triple-helical structural proteins that are ubiquitous in vertebrates. Improper folding of collagen can lead to disorders such as osteogenesis imperfecta, or "brittle bone disease." There is significant interest in understanding the factors that drive collagen folding and stability, but studying native collagens is difficult because they are hundreds of amino acids in length. This thesis describes a series of well-characterized (Pro-Hyp-Gly)7 model peptides which have been tagged at their N-termini with the fluorophore pyrene. When in close contact, pyrene units can form excimers that emit low-energy light. This allows for the study of several fundamental questions in collagen research using fluorescence spectroscopy, including concentration dependence, folding directionality, and local fraying, upon solutions that are significantly more dilute than those customarily used in circular dichroism (CD) experiments. Notably, for most of the peptides studied, there is agreement between the melting temperatures (Tm) obtained via fluorescence and CD techniques. In addition, the pyrene probes were found to provide a situational increase in thermal stability of triple helices.","abstract_has_math":false,"creators":["Keever, Jared Matthew"],"institution":"East Carolina University","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":"Chemistry","school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":["Burns, Colin Sanderson","Hudson, Nathan E","Sargent, Andrew L","Spuches, Anne M"],"year":2019,"date_issued":"2019-07-30","date_published":"2019-07-30","updated_at":"2026-07-24T02:13:51Z","subjects":["CD Spectrometry","Polyproline Helices","Stacking Interactions"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10342/7434","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Burns, Colin Sanderson","Hudson, Nathan E","Sargent, Andrew L","Spuches, Anne M"]},{"key":"dc:contributor.department","label":"Department","values":["Chemistry"]},{"key":"dc:creator","label":"Author","values":["Keever, Jared Matthew"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2019-08-21T16:03:25Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2020-12-01T09:01:55Z"]},{"key":"dc:date.issued","label":"Date","values":["2019-07-30"]},{"key":"dc:publisher","label":"Institution","values":["East Carolina University"]},{"key":"dc:type","label":"Dc Type","values":["Master's Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["CD Spectrometry","Polyproline Helices","Stacking Interactions"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10342/7434"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Collagens are a family of triple-helical structural proteins that are ubiquitous in vertebrates. Improper folding of collagen can lead to disorders such as osteogenesis imperfecta, or \"brittle bone disease.\" There is significant interest in understanding the factors that drive collagen folding and stability, but studying native collagens is difficult because they are hundreds of amino acids in length. This thesis describes a series of well-characterized (Pro-Hyp-Gly)7 model peptides which have been tagged at their N-termini with the fluorophore pyrene. When in close contact, pyrene units can form excimers that emit low-energy light. This allows for the study of several fundamental questions in collagen research using fluorescence spectroscopy, including concentration dependence, folding directionality, and local fraying, upon solutions that are significantly more dilute than those customarily used in circular dichroism (CD) experiments. Notably, for most of the peptides studied, there is agreement between the melting temperatures (Tm) obtained via fluorescence and CD techniques. In addition, the pyrene probes were found to provide a situational increase in thermal stability of triple helices."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Studying Collagen with PyrATS: Pyrene-Appended Trimeric Systems"]}]}],"canonical_facts":{"dc:contributor.committeemember":["Burns, Colin Sanderson","Hudson, Nathan E","Sargent, Andrew L","Spuches, Anne M"],"dc:contributor.department":["Chemistry"],"dc:creator":["Keever, Jared Matthew"],"dc:date.accessioned":["2019-08-21T16:03:25Z"],"dc:date.available":["2020-12-01T09:01:55Z"],"dc:date.issued":["2019-07-30"],"dc:description.abstract":["Collagens are a family of triple-helical structural proteins that are ubiquitous in vertebrates. Improper folding of collagen can lead to disorders such as osteogenesis imperfecta, or \"brittle bone disease.\" There is significant interest in understanding the factors that drive collagen folding and stability, but studying native collagens is difficult because they are hundreds of amino acids in length. This thesis describes a series of well-characterized (Pro-Hyp-Gly)7 model peptides which have been tagged at their N-termini with the fluorophore pyrene. When in close contact, pyrene units can form excimers that emit low-energy light. This allows for the study of several fundamental questions in collagen research using fluorescence spectroscopy, including concentration dependence, folding directionality, and local fraying, upon solutions that are significantly more dilute than those customarily used in circular dichroism (CD) experiments. Notably, for most of the peptides studied, there is agreement between the melting temperatures (Tm) obtained via fluorescence and CD techniques. In addition, the pyrene probes were found to provide a situational increase in thermal stability of triple helices."],"dc:format.mimetype":["application/pdf"],"dc:identifier.uri":["http://hdl.handle.net/10342/7434"],"dc:language.iso":["en"],"dc:publisher":["East Carolina University"],"dc:subject":["CD Spectrometry","Polyproline Helices","Stacking Interactions"],"dc:title":["Studying Collagen with PyrATS: Pyrene-Appended Trimeric Systems"],"dc:type":["Master's Thesis"]},"updated_at":"2026-07-24T02:13:51Z"}