{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/23939"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/23939","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Long lived states induced by extended illumination of carbonmonoxy-myoglobin","abstract":"\"Myoglobin is a heme-protein that binds small ligands, such as 02 and CO. A photon of visible light absorbed by the protein can break the protein ligand bond. At low temperatures (> 160K) the kinetics of recombination of photodissociated carbonmonoxymyoglobin are non-exponential, having amplitude components that extend over many orders of magnitude in time. The bound and unbound states of the system have different spectroscopic signatures and the kinetics of recombination can be measured by monitoring the time dependence of the absorption spectrum of the sample after photodissociation. After a period of intense illumination with light, the recombination kinetics slow down. The proteins are \"\"pumped\"\" to longer lived states. After waiting, the system resets, such that a photodissociation initiates regular, non-pumped, kinetics. I have measured the kinetics of the \"\"pumped\"\" states and the time course of the resetting, at various temperatures. Physical models, including connections to glass theories, are considered, and thermodynamic parameters for the various processes involved havebeen determined.\"","abstract_html":""Myoglobin is a heme-protein that binds small ligands, such as 02 and CO. A photon of visible light absorbed by the protein can break the protein ligand bond. At low temperatures (> 160K) the kinetics of recombination of photodissociated carbonmonoxymyoglobin are non-exponential, having amplitude components that extend over many orders of magnitude in time. The bound and unbound states of the system have different spectroscopic signatures and the kinetics of recombination can be measured by monitoring the time dependence of the absorption spectrum of the sample after photodissociation. After a period of intense illumination with light, the recombination kinetics slow down. The proteins are ""pumped"" to longer lived states. After waiting, the system resets, such that a photodissociation initiates regular, non-pumped, kinetics. I have measured the kinetics of the ""pumped"" states and the time course of the resetting, at various temperatures. Physical models, including connections to glass theories, are considered, and thermodynamic parameters for the various processes involved havebeen determined."","abstract_has_math":false,"creators":["Sauke, Todd Bennet"],"institution":null,"degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Physics","degree_department":null,"school":null,"contributors":["Frauenfelder, Hans"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-18T15:24:48Z","date_published":"2011-05-18T15:24:48Z","updated_at":"2026-07-22T22:25:22Z","subjects":["carbonmonoxymyoglobin","myoglobin","protein kinetics","ligand binding kinetics","recombination kinetics","illumination"],"languages":["en"],"rights":["1989 Todd Bennet Sauke"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["3478197"],"render_values":[{"text":"3478197","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/23939","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Frauenfelder, Hans"]},{"key":"dc:creator","label":"Author","values":["Sauke, Todd Bennet"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-18T15:24:48Z","10000-01-01","1989"]},{"key":"dc:type","label":"Dc Type","values":["Dissertation / Thesis","text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Physics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["carbonmonoxymyoglobin","myoglobin","protein kinetics","ligand binding kinetics","recombination kinetics","illumination"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["1989 Todd Bennet Sauke"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["3478197","http://hdl.handle.net/2142/23939"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["\"Myoglobin is a heme-protein that binds small ligands, such as 02 and CO. A photon of visible light absorbed by the protein can break the protein ligand bond. At low temperatures (> 160K) the kinetics of recombination of photodissociated carbonmonoxymyoglobin are non-exponential, having amplitude components that extend over many orders of magnitude in time. The bound and unbound states of the system have different spectroscopic signatures and the kinetics of recombination can be measured by monitoring the time dependence of the absorption spectrum of the sample after photodissociation. After a period of intense illumination with light, the recombination kinetics slow down. The proteins are \"\"pumped\"\" to longer lived states. After waiting, the system resets, such that a photodissociation initiates regular, non-pumped, kinetics. I have measured the kinetics of the \"\"pumped\"\" states and the time course of the resetting, at various temperatures. Physical models, including connections to glass theories, are considered, and thermodynamic parameters for the various processes involved havebeen determined.\"","Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-05-18T15:24:48Z No. of bitstreams: 1 1989_sauke.pdf: 6165754 bytes, checksum: 509e47c61372825f9aeeb321ff5ee62d (MD5)","Made available in DSpace on 2011-05-18T15:24:48Z (GMT). No. of bitstreams: 1 1989_sauke.pdf: 6165754 bytes, checksum: 509e47c61372825f9aeeb321ff5ee62d (MD5) Previous issue date: 1989","Restriction data tranferred 2014-07-01T11:13:43-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-05-18T15:24:48Z Item is restricted indefinitely.","Thesis","U of I Only"]},{"key":"dc:title","label":"Title","values":["Long lived states induced by extended illumination of carbonmonoxy-myoglobin"]}]}],"canonical_facts":{"dc:contributor":["Frauenfelder, Hans"],"dc:creator":["Sauke, Todd Bennet"],"dc:date":["2011-05-18T15:24:48Z","10000-01-01","1989"],"dc:description":["\"Myoglobin is a heme-protein that binds small ligands, such as 02 and CO. A photon of visible light absorbed by the protein can break the protein ligand bond. At low temperatures (> 160K) the kinetics of recombination of photodissociated carbonmonoxymyoglobin are non-exponential, having amplitude components that extend over many orders of magnitude in time. The bound and unbound states of the system have different spectroscopic signatures and the kinetics of recombination can be measured by monitoring the time dependence of the absorption spectrum of the sample after photodissociation. After a period of intense illumination with light, the recombination kinetics slow down. The proteins are \"\"pumped\"\" to longer lived states. After waiting, the system resets, such that a photodissociation initiates regular, non-pumped, kinetics. I have measured the kinetics of the \"\"pumped\"\" states and the time course of the resetting, at various temperatures. Physical models, including connections to glass theories, are considered, and thermodynamic parameters for the various processes involved havebeen determined.\"","Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-05-18T15:24:48Z No. of bitstreams: 1 1989_sauke.pdf: 6165754 bytes, checksum: 509e47c61372825f9aeeb321ff5ee62d (MD5)","Made available in DSpace on 2011-05-18T15:24:48Z (GMT). No. of bitstreams: 1 1989_sauke.pdf: 6165754 bytes, checksum: 509e47c61372825f9aeeb321ff5ee62d (MD5) Previous issue date: 1989","Restriction data tranferred 2014-07-01T11:13:43-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-05-18T15:24:48Z Item is restricted indefinitely.","Thesis","U of I Only"],"dc:identifier":["3478197","http://hdl.handle.net/2142/23939"],"dc:language":["en"],"dc:rights":["1989 Todd Bennet Sauke"],"dc:subject":["carbonmonoxymyoglobin","myoglobin","protein kinetics","ligand binding kinetics","recombination kinetics","illumination"],"dc:title":["Long lived states induced by extended illumination of carbonmonoxy-myoglobin"],"dc:type":["Dissertation / Thesis","text"],"thesis:degree_discipline":["Physics"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."]},"updated_at":"2026-07-22T22:25:22Z"}