{"id":{"repo_id":"wfu","oai_identifier":"oai:wakespace.lib.wfu.edu:10339/37251"},"canonical_url":"https://search.dev.ndltd.org/etd/wfu/oai:wakespace.lib.wfu.edu:10339/37251","repository":{"repo_id":"wfu","name":"Wake Forest University","base_url":"https://wakespace.lib.wfu.edu/oai/request"},"display":{"title":"Investigating the Role of Conformational Flexibility in tRNA Aminoacylation","abstract":"Proteins are dynamic macromolecules. According to Koshland's classical \"induced fit\" model of enzyme regulation, proteins have essential conformational flexibility for ligand binding, which promotes catalysis by structural rearrangement. Proteins undergo structural rearrangements to bind ligands, regulate access to a catalytic site, or release products. The energetic contribution of protein flexibility to catalysis is not well understood, despite numerous high resolution crystal structures available for numerous proteins bound with their corresponding ligands.","abstract_html":"Proteins are dynamic macromolecules. According to Koshland's classical "induced fit" model of enzyme regulation, proteins have essential conformational flexibility for ligand binding, which promotes catalysis by structural rearrangement. Proteins undergo structural rearrangements to bind ligands, regulate access to a catalytic site, or release products. The energetic contribution of protein flexibility to catalysis is not well understood, despite numerous high resolution crystal structures available for numerous proteins bound with their corresponding ligands.","abstract_has_math":false,"creators":["Banerjee, Papri"],"institution":"Wake Forest University","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2012,"date_issued":"2012","date_published":"2012","updated_at":"2026-07-27T22:01:27Z","subjects":[],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10339/37251","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Banerjee, Papri"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2012-06-12T08:35:42Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2014-06-12T08:30:07Z"]},{"key":"dc:date.issued","label":"Date","values":["2012"]},{"key":"dc:publisher","label":"Institution","values":["Wake Forest University"]},{"key":"dc:type","label":"Dc Type","values":["Dissertation"]}]},{"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.uri","label":"Identifier URI","values":["http://hdl.handle.net/10339/37251"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Proteins are dynamic macromolecules. According to Koshland's classical \"induced fit\" model of enzyme regulation, proteins have essential conformational flexibility for ligand binding, which promotes catalysis by structural rearrangement. Proteins undergo structural rearrangements to bind ligands, regulate access to a catalytic site, or release products. The energetic contribution of protein flexibility to catalysis is not well understood, despite numerous high resolution crystal structures available for numerous proteins bound with their corresponding ligands."]},{"key":"dc:title","label":"Title","values":["Investigating the Role of Conformational Flexibility in tRNA Aminoacylation"]}]}],"canonical_facts":{"dc:creator":["Banerjee, Papri"],"dc:date.accessioned":["2012-06-12T08:35:42Z"],"dc:date.available":["2014-06-12T08:30:07Z"],"dc:date.issued":["2012"],"dc:description.abstract":["Proteins are dynamic macromolecules. According to Koshland's classical \"induced fit\" model of enzyme regulation, proteins have essential conformational flexibility for ligand binding, which promotes catalysis by structural rearrangement. Proteins undergo structural rearrangements to bind ligands, regulate access to a catalytic site, or release products. The energetic contribution of protein flexibility to catalysis is not well understood, despite numerous high resolution crystal structures available for numerous proteins bound with their corresponding ligands."],"dc:identifier.uri":["http://hdl.handle.net/10339/37251"],"dc:language.iso":["en"],"dc:publisher":["Wake Forest University"],"dc:title":["Investigating the Role of Conformational Flexibility in tRNA Aminoacylation"],"dc:type":["Dissertation"]},"updated_at":"2026-07-27T22:01:27Z"}