{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/23055"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/23055","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 O$\\sb2$ and CO. A photon of visible light absorbed by the protein can break the protein ligand bond. At low temperatures ($>$160K) the kinetics of recombination of photodissociated carbonmonoxy-myoglobin are non-exponential, having amplitude components that extend over many orders of magnitude in time. The bound and unbound states of the system have different spectroscopic signatures and the kinetics of recombination can be measured by monitoring the time dependence of the absorption spectrum of the sample after photodissociation.","abstract_html":"Myoglobin is a heme-protein that binds small ligands, such as O$\\sb2$ 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 carbonmonoxy-myoglobin 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.","abstract_has_math":true,"creators":["Sauke, Todd Bennet"],"institution":"University of Illinois at Urbana-Champaign","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":"2011-05-07T14:00:32Z","date_published":"2011-05-07T14:00:32Z","updated_at":"2026-07-22T22:25:21Z","subjects":["Physics, Molecular"],"languages":["eng"],"rights":["Copyright 1989 Sauke, Todd Bennet"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI8924937","(UMI)AAI8924937"],"render_values":[{"text":"AAI8924937","href":null,"code":true},{"text":"(UMI)AAI8924937","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/23055","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":["2011-05-07T14:00:32Z","10000-01-01","1989"]},{"key":"dc:type","label":"Dc Type","values":["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."]},{"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":["Physics, Molecular"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1989 Sauke, Todd Bennet"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI8924937","(UMI)AAI8924937","http://hdl.handle.net/2142/23055"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Myoglobin is a heme-protein that binds small ligands, such as O$\\sb2$ 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 carbonmonoxy-myoglobin 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 have been determined.\"","Made available in DSpace on 2011-05-07T14:00:32Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 8924937.pdf: 3192162 bytes, checksum: 0ba92fe313ff6a1481b99745954866db (MD5) Previous issue date: 1989","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T15:01:52Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:29:23-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","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":["2011-05-07T14:00:32Z","10000-01-01","1989"],"dc:description":["Myoglobin is a heme-protein that binds small ligands, such as O$\\sb2$ 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 carbonmonoxy-myoglobin 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 have been determined.\"","Made available in DSpace on 2011-05-07T14:00:32Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 8924937.pdf: 3192162 bytes, checksum: 0ba92fe313ff6a1481b99745954866db (MD5) Previous issue date: 1989","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T15:01:52Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:29:23-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"],"dc:identifier":["AAI8924937","(UMI)AAI8924937","http://hdl.handle.net/2142/23055"],"dc:language":["eng"],"dc:rights":["Copyright 1989 Sauke, Todd Bennet"],"dc:subject":["Physics, Molecular"],"dc:title":["Long-lived states induced by extended illumination of carbonmonoxy-myoglobin"],"dc:type":["text"],"thesis:degree_discipline":["Physics"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:21Z"}