{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84058"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84058","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Rational Design of Chemotherapeutic Agents by Quantitative Structure-Activity Relationships and Solution NMR Methods for High Resolution Protein Structure Refinement","abstract":"Second, work towards the study of solution protein structure refinement methods by high-resolution multi-dimensional nuclear magnetic resonance (NMR) spectroscopy is discussed. Uniformly 13C, 15N-labeled Saccharomyces cerevisiae iso-1 cytochrome c was overexpressed in Escherichia coli and purified in its ferric form for NMR studies. The chemical shifts of most of the 1H, 13C, and 15N nuclei were assigned for future analyses of the incorporation of 13Calpha chemical shift, 13Calpha chemical shift anisotropy, and residual dipolar coupling in the structure refinement calculation. The ultimate goal is the determination of a refinement method that includes the most effective combination of the types of restraints that will yield the most highly resolved protein structures. This will then have applications to structure-based methods of drug design, which rely upon the structure of the target enzyme and will complement the ligand-based method referred to above.","abstract_html":"Second, work towards the study of solution protein structure refinement methods by high-resolution multi-dimensional nuclear magnetic resonance (NMR) spectroscopy is discussed. Uniformly 13C, 15N-labeled Saccharomyces cerevisiae iso-1 cytochrome c was overexpressed in Escherichia coli and purified in its ferric form for NMR studies. The chemical shifts of most of the 1H, 13C, and 15N nuclei were assigned for future analyses of the incorporation of 13Calpha chemical shift, 13Calpha chemical shift anisotropy, and residual dipolar coupling in the structure refinement calculation. The ultimate goal is the determination of a refinement method that includes the most effective combination of the types of restraints that will yield the most highly resolved protein structures. This will then have applications to structure-based methods of drug design, which rely upon the structure of the target enzyme and will complement the ligand-based method referred to above.","abstract_has_math":false,"creators":["Szabo, Christina Miki"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Oldfield, Eric"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:12:39Z","date_published":"2015-09-25T22:12:39Z","updated_at":"2026-07-22T22:26:22Z","subjects":["Biophysics, General"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3030482"],"render_values":[{"text":"(MiAaPQ)AAI3030482","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84058","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Oldfield, Eric"]},{"key":"dc:creator","label":"Author","values":["Szabo, Christina Miki"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:12:39Z","10000-01-01","2001"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"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/2142/84058","(MiAaPQ)AAI3030482"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Second, work towards the study of solution protein structure refinement methods by high-resolution multi-dimensional nuclear magnetic resonance (NMR) spectroscopy is discussed. 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Uniformly 13C, 15N-labeled Saccharomyces cerevisiae iso-1 cytochrome c was overexpressed in Escherichia coli and purified in its ferric form for NMR studies. The chemical shifts of most of the 1H, 13C, and 15N nuclei were assigned for future analyses of the incorporation of 13Calpha chemical shift, 13Calpha chemical shift anisotropy, and residual dipolar coupling in the structure refinement calculation. The ultimate goal is the determination of a refinement method that includes the most effective combination of the types of restraints that will yield the most highly resolved protein structures. This will then have applications to structure-based methods of drug design, which rely upon the structure of the target enzyme and will complement the ligand-based method referred to above.","Made available in DSpace on 2015-09-25T22:12:39Z (GMT). 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