{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84056"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84056","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Early Events in the Folding of the Protein Ubiquitin","abstract":"The equilibrium and non-equilibrium behavior of several mutants of the small single-domain protein ubiquitin have been characterized, with an eye towards describing the early folding events. These events have been interrogated by a fast laser temperature-jump technique and by low temperature stopped flow mixing. In the case of the T-Jump, initially cold denatured protein solution is rapidly heated with a 20 nsec heating pulse. The subsequent refolding is monitored by time resolved fluorescence lifetime and spectrum. In the case of stopped flow mixing, an initially chemically denatured protein sample is diluted into a refolding buffer at temperatures as low as -20°. Here X-ray scattering, circular dichroism, and fluorescence intensity are followed as a function of time. The two techniques reveal two unexpected results. Non-exponential kinetics have been recorded in protein refolding studies for the first time, and a transient structure containing more alpha-helix than the native state has been observed during the protein's folding.","abstract_html":"The equilibrium and non-equilibrium behavior of several mutants of the small single-domain protein ubiquitin have been characterized, with an eye towards describing the early folding events. These events have been interrogated by a fast laser temperature-jump technique and by low temperature stopped flow mixing. In the case of the T-Jump, initially cold denatured protein solution is rapidly heated with a 20 nsec heating pulse. The subsequent refolding is monitored by time resolved fluorescence lifetime and spectrum. In the case of stopped flow mixing, an initially chemically denatured protein sample is diluted into a refolding buffer at temperatures as low as -20°. Here X-ray scattering, circular dichroism, and fluorescence intensity are followed as a function of time. The two techniques reveal two unexpected results. Non-exponential kinetics have been recorded in protein refolding studies for the first time, and a transient structure containing more alpha-helix than the native state has been observed during the protein's folding.","abstract_has_math":false,"creators":["Ervin, John Lawrence"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Martin Gruebele"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:12:38Z","date_published":"2015-09-25T22:12:38Z","updated_at":"2026-07-22T22:26:22Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3030429"],"render_values":[{"text":"(MiAaPQ)AAI3030429","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84056","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Martin Gruebele"]},{"key":"dc:creator","label":"Author","values":["Ervin, John Lawrence"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:12:38Z","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":["Chemistry, Biochemistry"]}]},{"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/2142/84056","(MiAaPQ)AAI3030429"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The equilibrium and non-equilibrium behavior of several mutants of the small single-domain protein ubiquitin have been characterized, with an eye towards describing the early folding events. These events have been interrogated by a fast laser temperature-jump technique and by low temperature stopped flow mixing. In the case of the T-Jump, initially cold denatured protein solution is rapidly heated with a 20 nsec heating pulse. The subsequent refolding is monitored by time resolved fluorescence lifetime and spectrum. In the case of stopped flow mixing, an initially chemically denatured protein sample is diluted into a refolding buffer at temperatures as low as -20°. Here X-ray scattering, circular dichroism, and fluorescence intensity are followed as a function of time. The two techniques reveal two unexpected results. Non-exponential kinetics have been recorded in protein refolding studies for the first time, and a transient structure containing more alpha-helix than the native state has been observed during the protein's folding.","Made available in DSpace on 2015-09-25T22:12:38Z (GMT). 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These events have been interrogated by a fast laser temperature-jump technique and by low temperature stopped flow mixing. In the case of the T-Jump, initially cold denatured protein solution is rapidly heated with a 20 nsec heating pulse. The subsequent refolding is monitored by time resolved fluorescence lifetime and spectrum. In the case of stopped flow mixing, an initially chemically denatured protein sample is diluted into a refolding buffer at temperatures as low as -20°. Here X-ray scattering, circular dichroism, and fluorescence intensity are followed as a function of time. The two techniques reveal two unexpected results. Non-exponential kinetics have been recorded in protein refolding studies for the first time, and a transient structure containing more alpha-helix than the native state has been observed during the protein's folding.","Made available in DSpace on 2015-09-25T22:12:38Z (GMT). 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