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- W2523208744 abstract "Heme c containing proteins are known for theirintense colors and essential functions in nature. These proteinscontain heme that is covalently bound to the protein. For part ofthe work in this thesis, we have developed fusion tags thatcontain heme c, known as heme-tags, that reversibly bind anL-histidine immobilized Sepharose (HIS) chromatography resin foraffinity purification of recombinant proteins expressed inEscherichia coli. The heme-tag HIS purification method couples theease of affinity purification with the convenience of visibledetection for protein tracking. In addition, we show that theheme-tag can be used to quantify the protein. Heme is covalentlybound to native heme c proteins by several dedicated biogenesissystems that exhibit a variable degree of diversity and substratespecificity. Heme-tagged proteins are produced using a biogenesissystem native to E. coli with promiscuous substrate specificity.The biogenesis system that matures native mitochondrialcytochromes c (cyt c) that function in cellular respiration andapoptosis is referred to as cytochrome c heme lyase (CCHL). Thesubstrate specificity of CCHL has been explored, but the detailsare unclear. In this thesis, we show that CCHL can mature thefirst 18 N-terminal residues of horse cyt c fused to a non-hemecontaining protein, which demonstrates that the C-terminal portionof cyt c is unimportant for substrate recognition. This work lendsnew insight into the substrate specificity of CCHL and provides anew approach for producing artificial heme c proteins that couldfind use in multiple applications. In addition to developing novelbiochemical applications of the heme tag, we study the folding ofthe important model protein horse cyt c. Protein folding isconsidered one of the most confounding problems in science, and cytc has long been a model protein to understand the generalprinciples of folding. Herein, we show that the folding of cyt cis more complex than previously reported using single moleculefluorescence methods. We show evidence of multiple foldingintermediates and pathways as the protein folds on its energylandscape." @default.
- W2523208744 created "2016-09-30" @default.
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- W2523208744 date "2012-01-01" @default.
- W2523208744 modified "2023-09-24" @default.
- W2523208744 title "Engineering Native and Artificial Heme c Containing Proteins for Biochemical Applications and Studies of Protein Folding" @default.
- W2523208744 hasPublicationYear "2012" @default.
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