{"id":{"repo_id":"unm","oai_identifier":"oai:digitalrepository.unm.edu:nsms_etds-1010"},"canonical_url":"https://search.dev.ndltd.org/etd/unm/oai:digitalrepository.unm.edu:nsms_etds-1010","repository":{"repo_id":"unm","name":"University of New Mexico","base_url":"https://digitalrepository.unm.edu/do/oai/"},"display":{"title":"EVOLUTION AND CHARACTERIZATION OF A NEW REVERSIBLY PHOTOSWITCHABLE CHROMOPROTEIN","abstract":"We report the molecular engineering and spectral characterization of a new reversibly photoswitchable chromoprotein, B11 a variant of thermostable green protein (TGP) that has been evolved for favorable solubility, thermostability, and enhanced crystallization properties. Its 2.5 \\xc5 joint X-ray and neutron structure shows the location of critical hydrogen atoms, and reveals the position, orientation, and protonation states of solvent molecules in the chromophore and surrounding amino acids, which have not been ascertained to date from current X-ray structures. We report 1.65 \\xc5 ground state and light-induced state X-ray crystal structures of B11, which differs from TGP by four amino acids and has a weak fluorescence in its ground state, and these structures are compared to the wild-type TGP structure. These structures will enhance future engineering of new and novel fluorescent proteins.","abstract_html":"We report the molecular engineering and spectral characterization of a new reversibly photoswitchable chromoprotein, B11 a variant of thermostable green protein (TGP) that has been evolved for favorable solubility, thermostability, and enhanced crystallization properties. Its 2.5 \\xc5 joint X-ray and neutron structure shows the location of critical hydrogen atoms, and reveals the position, orientation, and protonation states of solvent molecules in the chromophore and surrounding amino acids, which have not been ascertained to date from current X-ray structures. We report 1.65 \\xc5 ground state and light-induced state X-ray crystal structures of B11, which differs from TGP by four amino acids and has a weak fluorescence in its ground state, and these structures are compared to the wild-type TGP structure. These structures will enhance future engineering of new and novel fluorescent proteins.","abstract_has_math":false,"creators":["Langan, Patricia"],"institution":null,"degree_name":"Nanoscience and Microsystems","degree_level":"Dissertation","degree_discipline":"Nanoscience and Microsystems","degree_department":null,"school":null,"contributors":["Freyer, James","Bradbury, Andrew","Lidke, Diane","Houston, Jessica"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-09-12T07:00:00Z","date_published":"2014-09-12T07:00:00Z","updated_at":"2026-07-24T05:26:42Z","subjects":["photoswitching","chromoprotein"],"languages":["English"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["https://digitalrepository.unm.edu/nsms_etds/11"],"render_values":[{"text":"https://digitalrepository.unm.edu/nsms_etds/11","href":"https://digitalrepository.unm.edu/nsms_etds/11","code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/1928/24571","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Freyer, James","Bradbury, Andrew","Lidke, Diane","Houston, Jessica"]},{"key":"dc:creator","label":"Author","values":["Langan, Patricia"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2016-07-26T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Nanoscience and Microsystems"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation","Doctoral"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Nanoscience and Microsystems"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["photoswitching","chromoprotein"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/1928/24571","https://digitalrepository.unm.edu/nsms_etds/11"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["We report the molecular engineering and spectral characterization of a new reversibly photoswitchable chromoprotein, B11 a variant of thermostable green protein (TGP) that has been evolved for favorable solubility, thermostability, and enhanced crystallization properties. Its 2.5 \\xc5 joint X-ray and neutron structure shows the location of critical hydrogen atoms, and reveals the position, orientation, and protonation states of solvent molecules in the chromophore and surrounding amino acids, which have not been ascertained to date from current X-ray structures. We report 1.65 \\xc5 ground state and light-induced state X-ray crystal structures of B11, which differs from TGP by four amino acids and has a weak fluorescence in its ground state, and these structures are compared to the wild-type TGP structure. These structures will enhance future engineering of new and novel fluorescent proteins."]},{"key":"dc:title","label":"Title","values":["EVOLUTION AND CHARACTERIZATION OF A NEW REVERSIBLY PHOTOSWITCHABLE CHROMOPROTEIN"]}]}],"canonical_facts":{"dc:contributor":["Freyer, James","Bradbury, Andrew","Lidke, Diane","Houston, Jessica"],"dc:creator":["Langan, Patricia"],"dc:date.available":["2016-07-26T07:00:00Z"],"dc:description.abstract":["We report the molecular engineering and spectral characterization of a new reversibly photoswitchable chromoprotein, B11 a variant of thermostable green protein (TGP) that has been evolved for favorable solubility, thermostability, and enhanced crystallization properties. Its 2.5 \\xc5 joint X-ray and neutron structure shows the location of critical hydrogen atoms, and reveals the position, orientation, and protonation states of solvent molecules in the chromophore and surrounding amino acids, which have not been ascertained to date from current X-ray structures. We report 1.65 \\xc5 ground state and light-induced state X-ray crystal structures of B11, which differs from TGP by four amino acids and has a weak fluorescence in its ground state, and these structures are compared to the wild-type TGP structure. These structures will enhance future engineering of new and novel fluorescent proteins."],"dc:identifier":["http://hdl.handle.net/1928/24571","https://digitalrepository.unm.edu/nsms_etds/11"],"dc:language":["English"],"dc:subject":["photoswitching","chromoprotein"],"dc:title":["EVOLUTION AND CHARACTERIZATION OF A NEW REVERSIBLY PHOTOSWITCHABLE CHROMOPROTEIN"],"thesis:degree_discipline":["Nanoscience and Microsystems"],"thesis:degree_level":["Dissertation","Doctoral"],"thesis:degree_name":["Nanoscience and Microsystems"]},"updated_at":"2026-07-24T05:26:42Z"}