{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/77477"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/77477","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"General Features of Ligand Binding to Heme Proteins","abstract":"The binding of ligands to heme proteins has been studied extensively in the past. A sequential barrier model was postulated. Using flash photolysis, various aspects of the model are studied in this work to give a better understanding of ligand binding. Binding from the pocket, as seen at low temperatures as process I, is examined under the influence of xenon binding, pH, high ligand concentration and Zn('++) ions. A new approach is developed to understand binding at physiological temperatures. The effect of solvent is examined with the new approach. The role of diffusion in binding is discussed. Support for a sequential model and the existence of conformational substates are presented. The effect of high ligand concentration on the kinetics is also investigated.","abstract_html":"The binding of ligands to heme proteins has been studied extensively in the past. A sequential barrier model was postulated. Using flash photolysis, various aspects of the model are studied in this work to give a better understanding of ligand binding. Binding from the pocket, as seen at low temperatures as process I, is examined under the influence of xenon binding, pH, high ligand concentration and Zn('++) ions. A new approach is developed to understand binding at physiological temperatures. The effect of solvent is examined with the new approach. The role of diffusion in binding is discussed. Support for a sequential model and the existence of conformational substates are presented. The effect of high ligand concentration on the kinetics is also investigated.","abstract_has_math":false,"creators":["Yue, Kwok To"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biophysics","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-05-13T15:47:09Z","date_published":"2015-05-13T15:47:09Z","updated_at":"2026-07-22T22:26:10Z","subjects":["Biophysics, General"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8310023"],"render_values":[{"text":"(UMI)AAI8310023","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/77477","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Yue, Kwok To"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-05-13T15:47:09Z","10000-01-01","1983"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biophysics"]},{"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/2142/77477","(UMI)AAI8310023"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The binding of ligands to heme proteins has been studied extensively in the past. A sequential barrier model was postulated. Using flash photolysis, various aspects of the model are studied in this work to give a better understanding of ligand binding. Binding from the pocket, as seen at low temperatures as process I, is examined under the influence of xenon binding, pH, high ligand concentration and Zn('++) ions. A new approach is developed to understand binding at physiological temperatures. The effect of solvent is examined with the new approach. The role of diffusion in binding is discussed. Support for a sequential model and the existence of conformational substates are presented. The effect of high ligand concentration on the kinetics is also investigated.","Made available in DSpace on 2015-05-13T15:47:09Z (GMT). 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Using flash photolysis, various aspects of the model are studied in this work to give a better understanding of ligand binding. Binding from the pocket, as seen at low temperatures as process I, is examined under the influence of xenon binding, pH, high ligand concentration and Zn('++) ions. A new approach is developed to understand binding at physiological temperatures. The effect of solvent is examined with the new approach. The role of diffusion in binding is discussed. Support for a sequential model and the existence of conformational substates are presented. The effect of high ligand concentration on the kinetics is also investigated.","Made available in DSpace on 2015-05-13T15:47:09Z (GMT). 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