{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/85419"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/85419","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Mechanism of C -Cadherin Binding: Multiple Adhesive Alignments and a Multi-Stage Unbinding Trajectory","abstract":"A preliminary characterization of the structure of membrane supported C-cadherin monolayers, that are used in the surface force measurements, is presented in the latter part of the thesis. Using ellipsometry, we monitor the binding of C-cadherin to lipid monolayers in real time. These data suggest that in the presence of calcium, cadherin forms adhesive complexes on lipid monolayers, and these complexes are disrupted by calcium removal. Using x-ray reflectivity, we measure preliminary electron density profiles of the C-cadherin layers and their supporting lipids, normal to the air-water interface. These electron density profiles are used to estimate the dimensions of the cadherin and the lipid monolayers. The thickness of the lipid monolayer and the cadherin extracellular region measured using x-ray reflectivity shows a good agreement with the steric thickness of these layers determined by direct force measurements.","abstract_html":"A preliminary characterization of the structure of membrane supported C-cadherin monolayers, that are used in the surface force measurements, is presented in the latter part of the thesis. Using ellipsometry, we monitor the binding of C-cadherin to lipid monolayers in real time. These data suggest that in the presence of calcium, cadherin forms adhesive complexes on lipid monolayers, and these complexes are disrupted by calcium removal. Using x-ray reflectivity, we measure preliminary electron density profiles of the C-cadherin layers and their supporting lipids, normal to the air-water interface. These electron density profiles are used to estimate the dimensions of the cadherin and the lipid monolayers. The thickness of the lipid monolayer and the cadherin extracellular region measured using x-ray reflectivity shows a good agreement with the steric thickness of these layers determined by direct force measurements.","abstract_has_math":false,"creators":["Sivasankar, Sanjeevi"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biophysics and Computational Biology","degree_department":null,"school":null,"contributors":["Leckband, Deborah E."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:46:01Z","date_published":"2015-09-25T22:46:01Z","updated_at":"2026-07-22T22:26:25Z","subjects":["Engineering, Biomedical"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3017209"],"render_values":[{"text":"(MiAaPQ)AAI3017209","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/85419","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Leckband, Deborah E."]},{"key":"dc:creator","label":"Author","values":["Sivasankar, Sanjeevi"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:46:01Z","10000-01-01","2001"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biophysics and Computational Biology"]},{"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":["Engineering, Biomedical"]}]},{"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/2142/85419","(MiAaPQ)AAI3017209"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["A preliminary characterization of the structure of membrane supported C-cadherin monolayers, that are used in the surface force measurements, is presented in the latter part of the thesis. Using ellipsometry, we monitor the binding of C-cadherin to lipid monolayers in real time. These data suggest that in the presence of calcium, cadherin forms adhesive complexes on lipid monolayers, and these complexes are disrupted by calcium removal. Using x-ray reflectivity, we measure preliminary electron density profiles of the C-cadherin layers and their supporting lipids, normal to the air-water interface. These electron density profiles are used to estimate the dimensions of the cadherin and the lipid monolayers. The thickness of the lipid monolayer and the cadherin extracellular region measured using x-ray reflectivity shows a good agreement with the steric thickness of these layers determined by direct force measurements.","Made available in DSpace on 2015-09-25T22:46:01Z (GMT). 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Using ellipsometry, we monitor the binding of C-cadherin to lipid monolayers in real time. These data suggest that in the presence of calcium, cadherin forms adhesive complexes on lipid monolayers, and these complexes are disrupted by calcium removal. Using x-ray reflectivity, we measure preliminary electron density profiles of the C-cadherin layers and their supporting lipids, normal to the air-water interface. These electron density profiles are used to estimate the dimensions of the cadherin and the lipid monolayers. The thickness of the lipid monolayer and the cadherin extracellular region measured using x-ray reflectivity shows a good agreement with the steric thickness of these layers determined by direct force measurements.","Made available in DSpace on 2015-09-25T22:46:01Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3017209.pdf: 5273608 bytes, checksum: 870e218a03d41523ef3df371c1529820 (MD5) Previous issue date: 2001","Embargo set by: Seth Robbins for item 86700 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","119 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2001."],"dc:identifier":["http://hdl.handle.net/2142/85419","(MiAaPQ)AAI3017209"],"dc:language":["eng"],"dc:subject":["Engineering, Biomedical"],"dc:title":["Mechanism of C -Cadherin Binding: Multiple Adhesive Alignments and a Multi-Stage Unbinding Trajectory"],"dc:type":["text"],"thesis:degree_discipline":["Biophysics and Computational Biology"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:25Z"}