{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/87869"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/87869","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Effects of Immobilization Matrices and Protein Orientation on Biomolecular Recognition at Solid-Liquid Interfaces","abstract":"We then investigated the dependence of protein orientation on the forces between immobilized proteins and soluble ligands. Oriented cytochrome b5 monolayers were constructed on supported lipid membranes using a site-selective immobilization method. The orientation of the immobilized cytochrome b5 was well controlled as verified with linear dichroism measurements. The orientational dependence of the protein electrostatic surface potentials was observed by direct force measurement. The impact of immobilized cytochrome b5 orientation on the forces mediating the cytochrome b5-cytochrome c recognition was quantified, and correlated with the measured surface binding behaviors. We found good agreement between force measurements, molecular models, and equilibrium binding behavior.","abstract_html":"We then investigated the dependence of protein orientation on the forces between immobilized proteins and soluble ligands. Oriented cytochrome b5 monolayers were constructed on supported lipid membranes using a site-selective immobilization method. The orientation of the immobilized cytochrome b5 was well controlled as verified with linear dichroism measurements. The orientational dependence of the protein electrostatic surface potentials was observed by direct force measurement. The impact of immobilized cytochrome b5 orientation on the forces mediating the cytochrome b5-cytochrome c recognition was quantified, and correlated with the measured surface binding behaviors. We found good agreement between force measurements, molecular models, and equilibrium binding behavior.","abstract_has_math":false,"creators":["Yeung, Chiuman"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":null,"degree_department":null,"school":null,"contributors":["Leckband, Deborah E."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-28T21:56:27Z","date_published":"2015-09-28T21:56:27Z","updated_at":"2026-07-22T22:26:31Z","subjects":["Biophysics, General"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9904632"],"render_values":[{"text":"(MiAaPQ)AAI9904632","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/87869","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":["Yeung, Chiuman"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-28T21:56:27Z","10000-01-01","1998"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"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":["Biophysics, General"]}]},{"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/2142/87869","(MiAaPQ)AAI9904632"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["We then investigated the dependence of protein orientation on the forces between immobilized proteins and soluble ligands. Oriented cytochrome b5 monolayers were constructed on supported lipid membranes using a site-selective immobilization method. The orientation of the immobilized cytochrome b5 was well controlled as verified with linear dichroism measurements. The orientational dependence of the protein electrostatic surface potentials was observed by direct force measurement. The impact of immobilized cytochrome b5 orientation on the forces mediating the cytochrome b5-cytochrome c recognition was quantified, and correlated with the measured surface binding behaviors. We found good agreement between force measurements, molecular models, and equilibrium binding behavior.","Made available in DSpace on 2015-09-28T21:56:27Z (GMT). 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Oriented cytochrome b5 monolayers were constructed on supported lipid membranes using a site-selective immobilization method. The orientation of the immobilized cytochrome b5 was well controlled as verified with linear dichroism measurements. The orientational dependence of the protein electrostatic surface potentials was observed by direct force measurement. The impact of immobilized cytochrome b5 orientation on the forces mediating the cytochrome b5-cytochrome c recognition was quantified, and correlated with the measured surface binding behaviors. We found good agreement between force measurements, molecular models, and equilibrium binding behavior.","Made available in DSpace on 2015-09-28T21:56:27Z (GMT). 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