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oai:www.ideals.illinois.edu:2142/86722 2023-07-11 col_2142_5131 col_2142_16338 com_2142_5130 com_2142_16337 com_2142_14793 com_2142_8903

Konisky, Jordan Haney, Paul Jeffrey 2015-09-28T15:17:38Z 2015-09-28T15:17:38Z 10000-01-01 1997 1997 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). 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. http://hdl.handle.net/2142/86722 (MiAaPQ)AAI9812611 eng Chemistry, Biochemistry Investigation of Adenylate Kinases Isolated From Mesophilic and Thermophilic Members of the Archaeal Genus Methanococcus text Microbiology Microbiology University of Illinois at Urbana-Champaign Dissertation Ph.D.