{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/86722"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/86722","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Investigation of Adenylate Kinases Isolated From Mesophilic and Thermophilic Members of the Archaeal Genus Methanococcus","abstract":"Construction of chimeric proteins between M. voltae and M. jannaschii AKs along with site specific mutational analysis confirm the importance of specific stabilizing interactions identified by sequence comparisons, and allow the physical characteristic of these proteins to be significantly altered. Simple protein engineering increased the temperature optima of the Methanococcus voltae AK from 37$\\sp\\circ$C to 62$\\sp\\circ$C and its melting point from 68$\\sp\\circ$C to 89$\\sp\\circ$C while maintaining specific activity levels and approximately 90% of its original sequence. Analysis of the chimerical proteins also point strongly to the cooperative and non-additive nature of thermal stabilizing interactions within the methanococcal AKs. These studies also indicate that the molecular mechanisms which determine enzymatic temperature optima and overall protein stability are not directly related.","abstract_html":"Construction of chimeric proteins between M. voltae and M. jannaschii AKs along with site specific mutational analysis confirm the importance of specific stabilizing interactions identified by sequence comparisons, and allow the physical characteristic of these proteins to be significantly altered. Simple protein engineering increased the temperature optima of the Methanococcus voltae AK from 37$\\sp\\circ$C to 62$\\sp\\circ$C and its melting point from 68$\\sp\\circ$C to 89$\\sp\\circ$C while maintaining specific activity levels and approximately 90% of its original sequence. Analysis of the chimerical proteins also point strongly to the cooperative and non-additive nature of thermal stabilizing interactions within the methanococcal AKs. These studies also indicate that the molecular mechanisms which determine enzymatic temperature optima and overall protein stability are not directly related.","abstract_has_math":true,"creators":["Haney, Paul Jeffrey"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Konisky, Jordan"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-28T15:17:38Z","date_published":"2015-09-28T15:17:38Z","updated_at":"2026-07-22T22:26:27Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9812611"],"render_values":[{"text":"(MiAaPQ)AAI9812611","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/86722","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Konisky, Jordan"]},{"key":"dc:creator","label":"Author","values":["Haney, Paul Jeffrey"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-28T15:17:38Z","10000-01-01","1997"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology"]},{"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/2142/86722","(MiAaPQ)AAI9812611"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Construction of chimeric proteins between M. voltae and M. jannaschii AKs along with site specific mutational analysis confirm the importance of specific stabilizing interactions identified by sequence comparisons, and allow the physical characteristic of these proteins to be significantly altered. Simple protein engineering increased the temperature optima of the Methanococcus voltae AK from 37$\\sp\\circ$C to 62$\\sp\\circ$C and its melting point from 68$\\sp\\circ$C to 89$\\sp\\circ$C while maintaining specific activity levels and approximately 90% of its original sequence. Analysis of the chimerical proteins also point strongly to the cooperative and non-additive nature of thermal stabilizing interactions within the methanococcal AKs. These studies also indicate that the molecular mechanisms which determine enzymatic temperature optima and overall protein stability are not directly related.","Made available in DSpace on 2015-09-28T15:17:38Z (GMT). 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Simple protein engineering increased the temperature optima of the Methanococcus voltae AK from 37$\\sp\\circ$C to 62$\\sp\\circ$C and its melting point from 68$\\sp\\circ$C to 89$\\sp\\circ$C while maintaining specific activity levels and approximately 90% of its original sequence. Analysis of the chimerical proteins also point strongly to the cooperative and non-additive nature of thermal stabilizing interactions within the methanococcal AKs. These studies also indicate that the molecular mechanisms which determine enzymatic temperature optima and overall protein stability are not directly related.","Made available in DSpace on 2015-09-28T15:17:38Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9812611.pdf: 5656724 bytes, checksum: 03f22a3b9b300e3a262233b154aeafe9 (MD5) Previous issue date: 1997","Embargo set by: Seth Robbins for item 88003 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","144 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1997."],"dc:identifier":["http://hdl.handle.net/2142/86722","(MiAaPQ)AAI9812611"],"dc:language":["eng"],"dc:subject":["Chemistry, Biochemistry"],"dc:title":["Investigation of Adenylate Kinases Isolated From Mesophilic and Thermophilic Members of the Archaeal Genus Methanococcus"],"dc:type":["text"],"thesis:degree_discipline":["Microbiology"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:27Z"}