{"id":{"repo_id":"texas","oai_identifier":"oai:repositories.lib.utexas.edu:2152/68037"},"canonical_url":"https://search.dev.ndltd.org/etd/texas/oai:repositories.lib.utexas.edu:2152/68037","repository":{"repo_id":"texas","name":"University of Texas","base_url":"https://repositories.lib.utexas.edu/server/oai/request"},"display":{"title":"Design, synthesis, and thermodynamic evaluation of peptidomimetic ligands binding to the Src SH2 domain","abstract":"The ability to predict protein-ligand binding affinities is a difficult and elusive goal in the field of molecular recognition. Models exist to predict binding energetics; however, they are not always capable of considering the incidental events in ligand-binding due to the tendency of the Gibbs free energy (ΔG°) to lack a correlation with enthalpy (ΔH°), entropy (ΔS°), or both. Binding studies of various pYEEI-derived peptidomimetic ligands to the Src SH2 domain were evaluated to investigate the effects of structural changes on protein-ligand binding energetics. The effect of preorganizing the pYEEI ligand into its binding conformation was analyzed by substituting the isoleucine residue with a conformationally constrained amino acid analog as well as a flexible analog. Isothermal titration calorimetry studies were performed to assess the effects of ligand structure on protein-ligand binding energetics.","abstract_html":"The ability to predict protein-ligand binding affinities is a difficult and elusive goal in the field of molecular recognition. Models exist to predict binding energetics; however, they are not always capable of considering the incidental events in ligand-binding due to the tendency of the Gibbs free energy (ΔG°) to lack a correlation with enthalpy (ΔH°), entropy (ΔS°), or both. Binding studies of various pYEEI-derived peptidomimetic ligands to the Src SH2 domain were evaluated to investigate the effects of structural changes on protein-ligand binding energetics. The effect of preorganizing the pYEEI ligand into its binding conformation was analyzed by substituting the isoleucine residue with a conformationally constrained amino acid analog as well as a flexible analog. Isothermal titration calorimetry studies were performed to assess the effects of ligand structure on protein-ligand binding energetics.","abstract_has_math":false,"creators":["Farley, Christopher Alexander"],"institution":"The University of Texas at Austin","degree_name":"Master of Arts","degree_level":"Masters","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":[],"advisors":["Martin, Stephen F."],"committee_chairs":[],"committee_members":[],"year":2018,"date_issued":"2018-05-03","date_published":"2018-05-03","updated_at":"2026-07-24T05:01:02Z","subjects":["Protein-ligand interactions","Protein-ligand binding","Ligand preorganization"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["doi:10.15781/T2X63BQ3N"],"render_values":[{"text":"doi:10.15781/T2X63BQ3N","href":"https://doi.org/10.15781/T2X63BQ3N","code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2152/68037","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Martin, Stephen F."]},{"key":"dc:creator","label":"Author","values":["Farley, Christopher Alexander"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2018-08-17T19:39:42Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2018-08-17T19:39:42Z"]},{"key":"dc:date.issued","label":"Date","values":["2018-05-03"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Arts"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["The University of Texas at Austin"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Protein-ligand interactions","Protein-ligand binding","Ligand preorganization"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["doi:10.15781/T2X63BQ3N"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/2152/68037"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The ability to predict protein-ligand binding affinities is a difficult and elusive goal in the field of molecular recognition. Models exist to predict binding energetics; however, they are not always capable of considering the incidental events in ligand-binding due to the tendency of the Gibbs free energy (ΔG°) to lack a correlation with enthalpy (ΔH°), entropy (ΔS°), or both. Binding studies of various pYEEI-derived peptidomimetic ligands to the Src SH2 domain were evaluated to investigate the effects of structural changes on protein-ligand binding energetics. The effect of preorganizing the pYEEI ligand into its binding conformation was analyzed by substituting the isoleucine residue with a conformationally constrained amino acid analog as well as a flexible analog. Isothermal titration calorimetry studies were performed to assess the effects of ligand structure on protein-ligand binding energetics."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Design, synthesis, and thermodynamic evaluation of peptidomimetic ligands binding to the Src SH2 domain"]}]}],"canonical_facts":{"dc:contributor.advisor":["Martin, Stephen F."],"dc:creator":["Farley, Christopher Alexander"],"dc:date.accessioned":["2018-08-17T19:39:42Z"],"dc:date.available":["2018-08-17T19:39:42Z"],"dc:date.issued":["2018-05-03"],"dc:description.abstract":["The ability to predict protein-ligand binding affinities is a difficult and elusive goal in the field of molecular recognition. Models exist to predict binding energetics; however, they are not always capable of considering the incidental events in ligand-binding due to the tendency of the Gibbs free energy (ΔG°) to lack a correlation with enthalpy (ΔH°), entropy (ΔS°), or both. Binding studies of various pYEEI-derived peptidomimetic ligands to the Src SH2 domain were evaluated to investigate the effects of structural changes on protein-ligand binding energetics. The effect of preorganizing the pYEEI ligand into its binding conformation was analyzed by substituting the isoleucine residue with a conformationally constrained amino acid analog as well as a flexible analog. Isothermal titration calorimetry studies were performed to assess the effects of ligand structure on protein-ligand binding energetics."],"dc:format.mimetype":["application/pdf"],"dc:identifier":["doi:10.15781/T2X63BQ3N"],"dc:identifier.uri":["http://hdl.handle.net/2152/68037"],"dc:language.iso":["en"],"dc:subject":["Protein-ligand interactions","Protein-ligand binding","Ligand preorganization"],"dc:title":["Design, synthesis, and thermodynamic evaluation of peptidomimetic ligands binding to the Src SH2 domain"],"dc:type":["Thesis"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Masters"],"thesis:degree_name":["Master of Arts"],"thesis:institution_name":["The University of Texas at Austin"]},"updated_at":"2026-07-24T05:01:02Z"}