{"id":{"repo_id":"purdue-thes","oai_identifier":"oai:docs.lib.purdue.edu:open_access_dissertations-1138"},"canonical_url":"https://search.dev.ndltd.org/etd/purdue-thes/oai:docs.lib.purdue.edu:open_access_dissertations-1138","repository":{"repo_id":"purdue-thes","name":"Purdue University","base_url":"https://docs.lib.purdue.edu/do/oai/"},"display":{"title":"Characterization of CAXCK31, a Bacterial Calcium/Proton Antiporter","abstract":"<p>To better understand a class of transporters known as Calcium/Cation Antiporters (CaCAs), the bacterial calcium/proton antiporter CAXCK31 was purified and characterized. New methods were developed for its heterologous overexpression and purification. These methods help to define stress responses to toxic membrane overproduction in E. coli and may be broadly applicable to studies of membrane proteins. The results from a variety of biochemical and biophysical experiments demonstrated that CAXCK31 exists as a dimer in the membrane and can be purified in the dimeric state. The methods used include chemical cross-linking, FRET, and SEC-MALS. In addition, various transport properties of CAXCK31, including substrate selectivity, pH dependence, and transport rates, have been characterized for the first time.</p>","abstract_html":"&lt;p&gt;To better understand a class of transporters known as Calcium/Cation Antiporters (CaCAs), the bacterial calcium/proton antiporter CAXCK31 was purified and characterized. New methods were developed for its heterologous overexpression and purification. These methods help to define stress responses to toxic membrane overproduction in E. coli and may be broadly applicable to studies of membrane proteins. The results from a variety of biochemical and biophysical experiments demonstrated that CAXCK31 exists as a dimer in the membrane and can be purified in the dimeric state. The methods used include chemical cross-linking, FRET, and SEC-MALS. In addition, various transport properties of CAXCK31, including substrate selectivity, pH dependence, and transport rates, have been characterized for the first time.&lt;/p&gt;","abstract_has_math":false,"creators":["Ridilla, Marc Robert"],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Dissertation","degree_discipline":"Biological Science","degree_department":null,"school":null,"contributors":["Jeffrey T. Bolin","Dinesh A. Yernool","Eric L. Baker","William A. Cramer"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2013,"date_issued":"2013-10-01T07:00:00Z","date_published":"2013-10-01T07:00:00Z","updated_at":"2026-07-24T03:53:11Z","subjects":["pure sciences","biological sciences","calcium","cation","antiporters","protons","Biochemistry","Biology","Molecular Biology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://docs.lib.purdue.edu/open_access_dissertations/76","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Jeffrey T. Bolin","Dinesh A. Yernool","Eric L. Baker","William A. 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New methods were developed for its heterologous overexpression and purification. These methods help to define stress responses to toxic membrane overproduction in E. coli and may be broadly applicable to studies of membrane proteins. The results from a variety of biochemical and biophysical experiments demonstrated that CAXCK31 exists as a dimer in the membrane and can be purified in the dimeric state. The methods used include chemical cross-linking, FRET, and SEC-MALS. In addition, various transport properties of CAXCK31, including substrate selectivity, pH dependence, and transport rates, have been characterized for the first time.</p>"]},{"key":"dc:title","label":"Title","values":["Characterization of CAXCK31, a Bacterial Calcium/Proton Antiporter"]}]}],"canonical_facts":{"dc:contributor":["Jeffrey T. Bolin","Dinesh A. Yernool","Eric L. Baker","William A. 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In addition, various transport properties of CAXCK31, including substrate selectivity, pH dependence, and transport rates, have been characterized for the first time.</p>"],"dc:identifier":["https://docs.lib.purdue.edu/open_access_dissertations/76"],"dc:subject":["pure sciences","biological sciences","calcium","cation","antiporters","protons","Biochemistry","Biology","Molecular Biology"],"dc:title":["Characterization of CAXCK31, a Bacterial Calcium/Proton Antiporter"],"thesis:degree_discipline":["Biological Science"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Doctor of Philosophy (PhD)"]},"updated_at":"2026-07-24T03:53:11Z"}