{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/77400"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/77400","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Infrared Studies of Rhodopsin, and Its Low Temperature Photoproducts, Bathorhodopsin and Isorhodopsin (Ftir, Vision)","abstract":"Fourier-transform infrared difference spectroscopy has been used to detect the vibrational modes of the chromophore and protein that change in position and intensity between rhodopsin and the photoproducts formed at low temperature (70K), bathorhodopsin and isorhodopsin. A method has been developed to obtain infrared difference spectra between rhodopsin and bathorhodopsin, bathorhodopsin and isorhodopsin, and rhodopsin and isorhodopsin. To aid in identification of the vibrational modes, experiments were performed on deuterated and hydrated films of native rod outer segments and rod outer segments regenerated with either retinal containing ('13)C at carbon-15 or 15-deuterioretinal, or hydrated films of rod outer segments regenerated with retinal containing ('13)C at either carbon-10, carbon-11, carbon-13, or carbons-14 and -15. These infrared studies provide independent verification of the resonance Raman result that the retinal in bathorhodopsin is all-trans-like. The positions of the C=N stretch in the deuterated pigment and the deuterated pigments regenerated with 1-cis 15-deuterioretinal or 11-cis containing ('13)C at carbon-15 are indicative that the Schiff base linkage is protonated in rhodopsin, bathorhodopsin, and isorhodopsin. Furthermore, the C=N stretching frequency occurs at the same position in all three species. The data indicate that the protonated Schiff base has a C=N trans conformation in all three species, and that the C10-C11 single bond is s-trans in bathorhodopsin. Finally, evidence is presented that, even in these early stages of the rhodopsin bleaching sequence, changes are occurring in the opsin.","abstract_html":"Fourier-transform infrared difference spectroscopy has been used to detect the vibrational modes of the chromophore and protein that change in position and intensity between rhodopsin and the photoproducts formed at low temperature (70K), bathorhodopsin and isorhodopsin. A method has been developed to obtain infrared difference spectra between rhodopsin and bathorhodopsin, bathorhodopsin and isorhodopsin, and rhodopsin and isorhodopsin. To aid in identification of the vibrational modes, experiments were performed on deuterated and hydrated films of native rod outer segments and rod outer segments regenerated with either retinal containing ('13)C at carbon-15 or 15-deuterioretinal, or hydrated films of rod outer segments regenerated with retinal containing ('13)C at either carbon-10, carbon-11, carbon-13, or carbons-14 and -15. These infrared studies provide independent verification of the resonance Raman result that the retinal in bathorhodopsin is all-trans-like. The positions of the C=N stretch in the deuterated pigment and the deuterated pigments regenerated with 1-cis 15-deuterioretinal or 11-cis containing ('13)C at carbon-15 are indicative that the Schiff base linkage is protonated in rhodopsin, bathorhodopsin, and isorhodopsin. Furthermore, the C=N stretching frequency occurs at the same position in all three species. The data indicate that the protonated Schiff base has a C=N trans conformation in all three species, and that the C10-C11 single bond is s-trans in bathorhodopsin. Finally, evidence is presented that, even in these early stages of the rhodopsin bleaching sequence, changes are occurring in the opsin.","abstract_has_math":false,"creators":["Bagley, Kimberly Ann"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Physics","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-05-13T15:41:54Z","date_published":"2015-05-13T15:41:54Z","updated_at":"2026-07-22T22:26:10Z","subjects":["Biophysics, General"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8711770"],"render_values":[{"text":"(UMI)AAI8711770","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/77400","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Bagley, Kimberly Ann"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-05-13T15:41:54Z","10000-01-01","1987"]},{"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":["Biophysics, General"]}]},{"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/2142/77400","(UMI)AAI8711770"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Fourier-transform infrared difference spectroscopy has been used to detect the vibrational modes of the chromophore and protein that change in position and intensity between rhodopsin and the photoproducts formed at low temperature (70K), bathorhodopsin and isorhodopsin. A method has been developed to obtain infrared difference spectra between rhodopsin and bathorhodopsin, bathorhodopsin and isorhodopsin, and rhodopsin and isorhodopsin. To aid in identification of the vibrational modes, experiments were performed on deuterated and hydrated films of native rod outer segments and rod outer segments regenerated with either retinal containing ('13)C at carbon-15 or 15-deuterioretinal, or hydrated films of rod outer segments regenerated with retinal containing ('13)C at either carbon-10, carbon-11, carbon-13, or carbons-14 and -15. These infrared studies provide independent verification of the resonance Raman result that the retinal in bathorhodopsin is all-trans-like. The positions of the C=N stretch in the deuterated pigment and the deuterated pigments regenerated with 1-cis 15-deuterioretinal or 11-cis containing ('13)C at carbon-15 are indicative that the Schiff base linkage is protonated in rhodopsin, bathorhodopsin, and isorhodopsin. Furthermore, the C=N stretching frequency occurs at the same position in all three species. The data indicate that the protonated Schiff base has a C=N trans conformation in all three species, and that the C10-C11 single bond is s-trans in bathorhodopsin. Finally, evidence is presented that, even in these early stages of the rhodopsin bleaching sequence, changes are occurring in the opsin.","Made available in DSpace on 2015-05-13T15:41:54Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 8711770.PDF: 3409232 bytes, checksum: 60240fd7afd5df5a25e497aba078ec1f (MD5) Previous issue date: 1987","Embargo set by: Seth Robbins for item 78611 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","128 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1987."]},{"key":"dc:title","label":"Title","values":["Infrared Studies of Rhodopsin, and Its Low Temperature Photoproducts, Bathorhodopsin and Isorhodopsin (Ftir, Vision)"]}]}],"canonical_facts":{"dc:creator":["Bagley, Kimberly Ann"],"dc:date":["2015-05-13T15:41:54Z","10000-01-01","1987"],"dc:description":["Fourier-transform infrared difference spectroscopy has been used to detect the vibrational modes of the chromophore and protein that change in position and intensity between rhodopsin and the photoproducts formed at low temperature (70K), bathorhodopsin and isorhodopsin. A method has been developed to obtain infrared difference spectra between rhodopsin and bathorhodopsin, bathorhodopsin and isorhodopsin, and rhodopsin and isorhodopsin. To aid in identification of the vibrational modes, experiments were performed on deuterated and hydrated films of native rod outer segments and rod outer segments regenerated with either retinal containing ('13)C at carbon-15 or 15-deuterioretinal, or hydrated films of rod outer segments regenerated with retinal containing ('13)C at either carbon-10, carbon-11, carbon-13, or carbons-14 and -15. These infrared studies provide independent verification of the resonance Raman result that the retinal in bathorhodopsin is all-trans-like. The positions of the C=N stretch in the deuterated pigment and the deuterated pigments regenerated with 1-cis 15-deuterioretinal or 11-cis containing ('13)C at carbon-15 are indicative that the Schiff base linkage is protonated in rhodopsin, bathorhodopsin, and isorhodopsin. Furthermore, the C=N stretching frequency occurs at the same position in all three species. The data indicate that the protonated Schiff base has a C=N trans conformation in all three species, and that the C10-C11 single bond is s-trans in bathorhodopsin. Finally, evidence is presented that, even in these early stages of the rhodopsin bleaching sequence, changes are occurring in the opsin.","Made available in DSpace on 2015-05-13T15:41:54Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 8711770.PDF: 3409232 bytes, checksum: 60240fd7afd5df5a25e497aba078ec1f (MD5) Previous issue date: 1987","Embargo set by: Seth Robbins for item 78611 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","128 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1987."],"dc:identifier":["http://hdl.handle.net/2142/77400","(UMI)AAI8711770"],"dc:language":["eng"],"dc:subject":["Biophysics, General"],"dc:title":["Infrared Studies of Rhodopsin, and Its Low Temperature Photoproducts, Bathorhodopsin and Isorhodopsin (Ftir, Vision)"],"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":"2026-07-22T22:26:10Z"}