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Sligar, Stephen G. Civjan, Natanya R. 2015-09-25T22:28:02Z 2015-09-25T22:28:02Z 10000-01-01 2005 2005 Whereas Arabidopsis P450s are typically membrane-associated, the hydrophobic nature of membrane-binding regions oftentimes creates difficulties in the solubilization, isolation and study of these proteins using traditional biochemical techniques. Paralleling the study of individual P450s was the development of a biotechnique to transfer membrane proteins directly from partially fractionated cellular membranes into soluble nanostructures that contain a native-like membrane environment. The resulting system is conducible to many of the biochemical methodologies previously restricted to soluble proteins and adds another tool to aid in the characterizations of this important class of enzymes. Made available in DSpace on 2015-09-25T22:28:02Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3198956.pdf: 3062813 bytes, checksum: 9aec7566415475d3a0f60214b9c48bf8 (MD5) Previous issue date: 2005 Embargo set by: Seth Robbins for item 86096 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 118 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2005. http://hdl.handle.net/2142/84815 (MiAaPQ)AAI3198956 eng Chemistry, Biochemistry Regulation and Functionality of Stress-Induced Cytochrome P450 Monooxygenases: A Functional Genomics Approach text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.