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https://hdl.handle.net/2142/84499
Description
Title
Metalloprotein Design
Author(s)
Sigman, Jeffrey Allen
Issue Date
2000
Doctoral Committee Chair(s)
Lu, Yi
Department of Study
Chemistry
Discipline
Chemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
Abstract
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.
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