{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/85477"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/85477","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Ligand Binding and Structural Dynamics in C-Type Cytochromes","abstract":"The first molecular dynamic simulations of the interaction of cyt c and yeast bc1 complex are described. Contrary to results from crystallographic studies, the simulations reveal multiple dynamic hydrogen bonds and salt bridges in the cyt c-c 1 interface. A novel structural change in cyt c is also reported, involving residues 25--30, which may be responsible for cyt c destabilization. An interaction between cyt c1 monomers is proposed to be responsible for limiting the binding of cyt c to only one molecule per bc 1 dimer by altering the affinity of the cytochrome c binding site on the second cyt c1 monomer. A mechanism is also proposed explaining changes in cyt c binding affinity related to the position of the headgroup of the iron-sulfur protein.","abstract_html":"The first molecular dynamic simulations of the interaction of cyt c and yeast bc1 complex are described. Contrary to results from crystallographic studies, the simulations reveal multiple dynamic hydrogen bonds and salt bridges in the cyt c-c 1 interface. A novel structural change in cyt c is also reported, involving residues 25--30, which may be responsible for cyt c destabilization. An interaction between cyt c1 monomers is proposed to be responsible for limiting the binding of cyt c to only one molecule per bc 1 dimer by altering the affinity of the cytochrome c binding site on the second cyt c1 monomer. A mechanism is also proposed explaining changes in cyt c binding affinity related to the position of the headgroup of the iron-sulfur protein.","abstract_has_math":false,"creators":["Kokhan, Oleksandr"],"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":["Wraight, Colin A."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:46:13Z","date_published":"2015-09-25T22:46:13Z","updated_at":"2026-07-22T22:26:25Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3392097"],"render_values":[{"text":"(MiAaPQ)AAI3392097","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/85477","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Wraight, Colin A."]},{"key":"dc:creator","label":"Author","values":["Kokhan, Oleksandr"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:46:13Z","10000-01-01","2009"]},{"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":["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/2142/85477","(MiAaPQ)AAI3392097"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The first molecular dynamic simulations of the interaction of cyt c and yeast bc1 complex are described. Contrary to results from crystallographic studies, the simulations reveal multiple dynamic hydrogen bonds and salt bridges in the cyt c-c 1 interface. A novel structural change in cyt c is also reported, involving residues 25--30, which may be responsible for cyt c destabilization. An interaction between cyt c1 monomers is proposed to be responsible for limiting the binding of cyt c to only one molecule per bc 1 dimer by altering the affinity of the cytochrome c binding site on the second cyt c1 monomer. A mechanism is also proposed explaining changes in cyt c binding affinity related to the position of the headgroup of the iron-sulfur protein.","Made available in DSpace on 2015-09-25T22:46:13Z (GMT). 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Contrary to results from crystallographic studies, the simulations reveal multiple dynamic hydrogen bonds and salt bridges in the cyt c-c 1 interface. A novel structural change in cyt c is also reported, involving residues 25--30, which may be responsible for cyt c destabilization. An interaction between cyt c1 monomers is proposed to be responsible for limiting the binding of cyt c to only one molecule per bc 1 dimer by altering the affinity of the cytochrome c binding site on the second cyt c1 monomer. A mechanism is also proposed explaining changes in cyt c binding affinity related to the position of the headgroup of the iron-sulfur protein.","Made available in DSpace on 2015-09-25T22:46:13Z (GMT). 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