{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/82423"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/82423","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Molecular Mechanisms of Cell Adhesion","abstract":"NCAM forms a complex between its terminal domains Ig1 and Ig2. When NCAM of cell A and cell B connect to each other through complexes Ig12(A)/Ig12(B), the relative mobility of cells A and B and membrane tension exerts a force on the Ig12(A)/Ig12(B) complex. Here we investigate the response of the complex to force, using steered molecular dynamics. Starting from the structure of the complex from the Ig1-Ig2-Ig3 fragment, we first equilibrate the complex in solvent and show that its actual end-to-end length is markedly larger than in the crystal structure. We then show that the Ig12/Ig12 complex can behave as a molecular spring of spring constant ∼0.03 N/m in response to forces of tens of pico-Newton. Such tertiary structure elasticity can be expected to be pervasive considering the large number of multi-modular CAMs. Finally, we rupture the complex using higher forces to identify E16, F19, K98, and L175 as key residues stabilizing the complex.","abstract_html":"NCAM forms a complex between its terminal domains Ig1 and Ig2. When NCAM of cell A and cell B connect to each other through complexes Ig12(A)/Ig12(B), the relative mobility of cells A and B and membrane tension exerts a force on the Ig12(A)/Ig12(B) complex. Here we investigate the response of the complex to force, using steered molecular dynamics. Starting from the structure of the complex from the Ig1-Ig2-Ig3 fragment, we first equilibrate the complex in solvent and show that its actual end-to-end length is markedly larger than in the crystal structure. We then show that the Ig12/Ig12 complex can behave as a molecular spring of spring constant ∼0.03 N/m in response to forces of tens of pico-Newton. Such tertiary structure elasticity can be expected to be pervasive considering the large number of multi-modular CAMs. Finally, we rupture the complex using higher forces to identify E16, F19, K98, and L175 as key residues stabilizing the complex.","abstract_has_math":false,"creators":["Maruthamuthu, Venkat"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemical Engineering","degree_department":null,"school":null,"contributors":["Leckband, Deborah E."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T20:43:58Z","date_published":"2015-09-25T20:43:58Z","updated_at":"2026-07-22T22:26:18Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3363031"],"render_values":[{"text":"(MiAaPQ)AAI3363031","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/82423","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":["Maruthamuthu, Venkat"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T20:43:58Z","10000-01-01","2009"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemical Engineering"]},{"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":["Chemistry, Biochemistry"]}]},{"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/2142/82423","(MiAaPQ)AAI3363031"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["NCAM forms a complex between its terminal domains Ig1 and Ig2. When NCAM of cell A and cell B connect to each other through complexes Ig12(A)/Ig12(B), the relative mobility of cells A and B and membrane tension exerts a force on the Ig12(A)/Ig12(B) complex. Here we investigate the response of the complex to force, using steered molecular dynamics. Starting from the structure of the complex from the Ig1-Ig2-Ig3 fragment, we first equilibrate the complex in solvent and show that its actual end-to-end length is markedly larger than in the crystal structure. We then show that the Ig12/Ig12 complex can behave as a molecular spring of spring constant ∼0.03 N/m in response to forces of tens of pico-Newton. Such tertiary structure elasticity can be expected to be pervasive considering the large number of multi-modular CAMs. Finally, we rupture the complex using higher forces to identify E16, F19, K98, and L175 as key residues stabilizing the complex.","Made available in DSpace on 2015-09-25T20:43:58Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3363031.pdf: 3996524 bytes, checksum: 87d145e91f91a0fe627c480dcbd77bda (MD5) Previous issue date: 2009","Embargo set by: Seth Robbins for item 83704 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","151 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2009."]},{"key":"dc:title","label":"Title","values":["Molecular Mechanisms of Cell Adhesion"]}]}],"canonical_facts":{"dc:contributor":["Leckband, Deborah E."],"dc:creator":["Maruthamuthu, Venkat"],"dc:date":["2015-09-25T20:43:58Z","10000-01-01","2009"],"dc:description":["NCAM forms a complex between its terminal domains Ig1 and Ig2. When NCAM of cell A and cell B connect to each other through complexes Ig12(A)/Ig12(B), the relative mobility of cells A and B and membrane tension exerts a force on the Ig12(A)/Ig12(B) complex. Here we investigate the response of the complex to force, using steered molecular dynamics. Starting from the structure of the complex from the Ig1-Ig2-Ig3 fragment, we first equilibrate the complex in solvent and show that its actual end-to-end length is markedly larger than in the crystal structure. We then show that the Ig12/Ig12 complex can behave as a molecular spring of spring constant ∼0.03 N/m in response to forces of tens of pico-Newton. Such tertiary structure elasticity can be expected to be pervasive considering the large number of multi-modular CAMs. Finally, we rupture the complex using higher forces to identify E16, F19, K98, and L175 as key residues stabilizing the complex.","Made available in DSpace on 2015-09-25T20:43:58Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3363031.pdf: 3996524 bytes, checksum: 87d145e91f91a0fe627c480dcbd77bda (MD5) Previous issue date: 2009","Embargo set by: Seth Robbins for item 83704 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","151 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2009."],"dc:identifier":["http://hdl.handle.net/2142/82423","(MiAaPQ)AAI3363031"],"dc:language":["eng"],"dc:subject":["Chemistry, Biochemistry"],"dc:title":["Molecular Mechanisms of Cell Adhesion"],"dc:type":["text"],"thesis:degree_discipline":["Chemical Engineering"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:18Z"}