{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84361"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84361","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"High Pressure Effects on the Dynamics and Kinetics of Two Model Biochemical Systems","abstract":"Pressure effects on rate constants for hydrogen exchange between N-methylacetamide (NMA) and water were measured at pressures up to 5 kbar at three different pH values and temperatures using proton/nitrogen-14 decoupled NMR inversion transfer, and the apparent activation volumes of exchange determined. Hydrogen exchange between NMA and water serves as a model for amide-water hydrogen exchange in peptides and proteins which is sensitive to the local environment of the protons and is used to probe fluctuations in the local conformations of proteins. Hydrogen exchange rate constants were also measured as a function of concentration and pH at ambient pressure at each temperature, and the rate constants of the acid-, base-, and uncatalyzed hydrogen exchange reactions determined. With these values, activation volumes of the acid-, base-, and uncatalyzed exchange reactions were calculated. This is the first time the uncatalyzed activation volume, which is required in hydrogen exchange studies of peptides and proteins at high pressures, had been determined. The temperature dependence of the activation volumes and the catalyzed rate constants was also examined.","abstract_html":"Pressure effects on rate constants for hydrogen exchange between N-methylacetamide (NMA) and water were measured at pressures up to 5 kbar at three different pH values and temperatures using proton/nitrogen-14 decoupled NMR inversion transfer, and the apparent activation volumes of exchange determined. Hydrogen exchange between NMA and water serves as a model for amide-water hydrogen exchange in peptides and proteins which is sensitive to the local environment of the protons and is used to probe fluctuations in the local conformations of proteins. Hydrogen exchange rate constants were also measured as a function of concentration and pH at ambient pressure at each temperature, and the rate constants of the acid-, base-, and uncatalyzed hydrogen exchange reactions determined. With these values, activation volumes of the acid-, base-, and uncatalyzed exchange reactions were calculated. This is the first time the uncatalyzed activation volume, which is required in hydrogen exchange studies of peptides and proteins at high pressures, had been determined. The temperature dependence of the activation volumes and the catalyzed rate constants was also examined.","abstract_has_math":false,"creators":["Mabry, Stephanie Ann"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Jonas, Jiri"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:14:06Z","date_published":"2015-09-25T22:14:06Z","updated_at":"2026-07-22T22:26:23Z","subjects":["Chemistry, Physical"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9717304"],"render_values":[{"text":"(MiAaPQ)AAI9717304","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84361","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Jonas, Jiri"]},{"key":"dc:creator","label":"Author","values":["Mabry, Stephanie Ann"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:14:06Z","10000-01-01","1997"]},{"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":["Chemistry, Physical"]}]},{"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/2142/84361","(MiAaPQ)AAI9717304"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Pressure effects on rate constants for hydrogen exchange between N-methylacetamide (NMA) and water were measured at pressures up to 5 kbar at three different pH values and temperatures using proton/nitrogen-14 decoupled NMR inversion transfer, and the apparent activation volumes of exchange determined. Hydrogen exchange between NMA and water serves as a model for amide-water hydrogen exchange in peptides and proteins which is sensitive to the local environment of the protons and is used to probe fluctuations in the local conformations of proteins. Hydrogen exchange rate constants were also measured as a function of concentration and pH at ambient pressure at each temperature, and the rate constants of the acid-, base-, and uncatalyzed hydrogen exchange reactions determined. With these values, activation volumes of the acid-, base-, and uncatalyzed exchange reactions were calculated. This is the first time the uncatalyzed activation volume, which is required in hydrogen exchange studies of peptides and proteins at high pressures, had been determined. The temperature dependence of the activation volumes and the catalyzed rate constants was also examined.","Made available in DSpace on 2015-09-25T22:14:06Z (GMT). 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Hydrogen exchange between NMA and water serves as a model for amide-water hydrogen exchange in peptides and proteins which is sensitive to the local environment of the protons and is used to probe fluctuations in the local conformations of proteins. Hydrogen exchange rate constants were also measured as a function of concentration and pH at ambient pressure at each temperature, and the rate constants of the acid-, base-, and uncatalyzed hydrogen exchange reactions determined. With these values, activation volumes of the acid-, base-, and uncatalyzed exchange reactions were calculated. This is the first time the uncatalyzed activation volume, which is required in hydrogen exchange studies of peptides and proteins at high pressures, had been determined. The temperature dependence of the activation volumes and the catalyzed rate constants was also examined.","Made available in DSpace on 2015-09-25T22:14:06Z (GMT). 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