{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/23844"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/23844","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Role of proximal residues in controlling CO binding reactions in myoglobin","abstract":"Restriction data tranferred 2014-07-01T11:32:19-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","abstract_html":"Restriction data tranferred 2014-07-01T11:32:19-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","abstract_has_math":false,"creators":["Chien, Ellen Yu-Lin Tsai"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biology, Molecular","degree_department":null,"school":null,"contributors":["Sligar, Stephen G."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T14:29:13Z","date_published":"2011-05-07T14:29:13Z","updated_at":"2026-07-22T22:25:22Z","subjects":["Biology, Molecular","Chemistry, Biochemistry","Biophysics, General"],"languages":["eng"],"rights":["Copyright 1996 Chien, Ellen Yu-Lin Tsai"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["9780591254273","AAI9717262","(UMI)AAI9717262"],"render_values":[{"text":"9780591254273","href":null,"code":true},{"text":"AAI9717262","href":null,"code":true},{"text":"(UMI)AAI9717262","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/23844","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Sligar, Stephen G."]},{"key":"dc:creator","label":"Author","values":["Chien, Ellen Yu-Lin Tsai"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T14:29:13Z","10000-01-01","1996"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology, Molecular","Chemistry, Biochemistry","Biophysics, General"]},{"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":["Biology, Molecular","Chemistry, Biochemistry","Biophysics, General"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1996 Chien, Ellen Yu-Lin Tsai"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["9780591254273","AAI9717262","(UMI)AAI9717262","http://hdl.handle.net/2142/23844"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Restriction data tranferred 2014-07-01T11:32:19-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only","Heme proteins are ubiquitous in biological systems and it is of interest to understand how the structure of various heme proteins determines their respective biological function. Using site-directed mutagenesis, the amino acids Leu89, Ser92, and His97 have been changed to understand why these residues are highly conserved in myoglobin across species, to elucidate the structural and functional roles played by these residues. These residues are shown to be participants in forming a hydrogen bonding network with the proximal histidine, His93. The effect of disrupting the hydrogen bonding interactions is examined via CO flash photolysis and resonance Raman spectroscopy. Furthermore, residues number 87 to 94 have been replaced by the amino acids in the respective locations in hemoglobin $\\beta$-chain (residues number 86 to 93) to examine the importance of the F-helix in controlling ligand binding in myoglobin and hemoglobin $\\beta$-chain. Based on the modeled structures of the mutants using CHARMM, and the evidence presented in this thesis, we propose that not only is the orientation of the proximal histidine important in controlling ligand binding to the heme, the dynamics of the F-helix also play an important role in controlling the inner barrier in myoglobin and hemoglobin.","In order to understand the structure-function relationships in proteins, it is important to have accurate structures. Proteins are not static entities. How does one determine if a given crystal structure is a good representation of the protein in solution? How does one obtain structural information when a protein does not lend itself to crystallization nor is it amenable to NMR structure determination? In this thesis, we have explored the possibility of using 4-fluorotryptophan as an electrostatic probe in myoglobin and hemoglobin to gain both electrostatic and structural information via $\\sp{19}$F-NMR. We show that the combination of the fluorine's chemical shift determined from the $\\sp{19}$F-NMR spectra of labeled proteins and the calculated chemical shielding using existing crystal structures can be used to gain structural and electrostatic information. This thesis demonstrates that this combination is a new avenue for structural analysis.","Made available in DSpace on 2011-05-07T14:29:13Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9717262.pdf: 5653350 bytes, checksum: 558d98d40357398d6553db78670368ab (MD5) Previous issue date: 1996","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T15:07:18Z Item is restricted indefinitely."]},{"key":"dc:title","label":"Title","values":["Role of proximal residues in controlling CO binding reactions in myoglobin"]}]}],"canonical_facts":{"dc:contributor":["Sligar, Stephen G."],"dc:creator":["Chien, Ellen Yu-Lin Tsai"],"dc:date":["2011-05-07T14:29:13Z","10000-01-01","1996"],"dc:description":["Restriction data tranferred 2014-07-01T11:32:19-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only","Heme proteins are ubiquitous in biological systems and it is of interest to understand how the structure of various heme proteins determines their respective biological function. Using site-directed mutagenesis, the amino acids Leu89, Ser92, and His97 have been changed to understand why these residues are highly conserved in myoglobin across species, to elucidate the structural and functional roles played by these residues. These residues are shown to be participants in forming a hydrogen bonding network with the proximal histidine, His93. The effect of disrupting the hydrogen bonding interactions is examined via CO flash photolysis and resonance Raman spectroscopy. Furthermore, residues number 87 to 94 have been replaced by the amino acids in the respective locations in hemoglobin $\\beta$-chain (residues number 86 to 93) to examine the importance of the F-helix in controlling ligand binding in myoglobin and hemoglobin $\\beta$-chain. Based on the modeled structures of the mutants using CHARMM, and the evidence presented in this thesis, we propose that not only is the orientation of the proximal histidine important in controlling ligand binding to the heme, the dynamics of the F-helix also play an important role in controlling the inner barrier in myoglobin and hemoglobin.","In order to understand the structure-function relationships in proteins, it is important to have accurate structures. Proteins are not static entities. How does one determine if a given crystal structure is a good representation of the protein in solution? How does one obtain structural information when a protein does not lend itself to crystallization nor is it amenable to NMR structure determination? In this thesis, we have explored the possibility of using 4-fluorotryptophan as an electrostatic probe in myoglobin and hemoglobin to gain both electrostatic and structural information via $\\sp{19}$F-NMR. We show that the combination of the fluorine's chemical shift determined from the $\\sp{19}$F-NMR spectra of labeled proteins and the calculated chemical shielding using existing crystal structures can be used to gain structural and electrostatic information. This thesis demonstrates that this combination is a new avenue for structural analysis.","Made available in DSpace on 2011-05-07T14:29:13Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9717262.pdf: 5653350 bytes, checksum: 558d98d40357398d6553db78670368ab (MD5) Previous issue date: 1996","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T15:07:18Z Item is restricted indefinitely."],"dc:identifier":["9780591254273","AAI9717262","(UMI)AAI9717262","http://hdl.handle.net/2142/23844"],"dc:language":["eng"],"dc:rights":["Copyright 1996 Chien, Ellen Yu-Lin Tsai"],"dc:subject":["Biology, Molecular","Chemistry, Biochemistry","Biophysics, General"],"dc:title":["Role of proximal residues in controlling CO binding reactions in myoglobin"],"dc:type":["text"],"thesis:degree_discipline":["Biology, Molecular","Chemistry, Biochemistry","Biophysics, General"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:22Z"}