2026-09-23T01:05:46Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/84499 2023-07-11 col_2142_5131 col_2142_14789 com_2142_5130 com_2142_14788 com_2142_8903

Lu, Yi Sigman, Jeffrey Allen 2015-09-25T22:14:49Z 2015-09-25T22:14:49Z 10000-01-01 2000 2000 CcP has been used as a template for the purpose of producing a protein model of cytochrome P450 (cyt P450), and both CcP and swMb have been used as templates for engineering metal-binding sites characteristic of the active site in cytochrome c oxidase (CcO). Spectroscopic characterization of the mutants will be presented and will demonstrate that new metal centers, with spectral properties similar to the native enzymes, have been successfully engineered in the protein models. This study represents an advance in the field of protein redesign by using protein models with scaffolds bearing no sequence or structural homology to the modeled systems. Furthermore, this work demonstrates the usefulness of these models in understanding secondary coordination effects at the metal-binding sites within proteins and in introducing new activity into the redesigned protein. Made available in DSpace on 2015-09-25T22:14:49Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9990139.pdf: 6799988 bytes, checksum: 54e17dff456d938c6341b5de2d3e9581 (MD5) Previous issue date: 2000 Embargo set by: Seth Robbins for item 85780 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 156 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000. http://hdl.handle.net/2142/84499 (MiAaPQ)AAI9990139 eng Chemistry, Biochemistry Metalloprotein Design text Chemistry Chemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.