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• W2053196265 abstract "Abstract A cell‐free protein synthesis system is a powerful tool with which unnatural amino acids can be introduced into polypeptide chains. Here, the authors describe unnatural amino acid probing in a wheat germ cell‐free translation system as a method for detecting the structural changes that occur in a cofactor binding protein on a conversion of the protein from an apo‐form to a holo‐form. The authors selected the FMN‐binding protein from Desulfovibrio vulgaris as a model protein. The apo‐form of the protein was synthesized efficiently in the absence of FMN. The purified apo‐form could be correctly converted to the holo‐form. Thus, the system could synthesize the active apo‐form. Gel filtration chromatography, analytical ultracentrifugation, and circular dichroism‐spectra studies suggested that the FMN‐binding site of the apo‐form is open as compared with the holo‐form. To confirm this idea, the unnatural amino acid probing was performed by incorporating 3‐azido‐ L ‐tyrosine at the Tyr35 residue in the FMN‐binding site. The authors optimized three steps in their system. The introduced 3‐azido‐ L ‐tyrosine residue was subjected to specific chemical modification by a fluorescein‐triarylphosphine derivative. The initial velocity of the apo‐form reaction was 20 fold faster than that of the holo‐form, demonstrating that the Tyr35 residue in the apo‐form is open to solvent. Proteins 2007. © 2007 Wiley‐Liss, Inc." @default.
• W2053196265 created "2016-06-24" @default.
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• W2053196265 date "2007-03-08" @default.
• W2053196265 modified "2023-10-17" @default.
• W2053196265 title "Detection of structural changes in a cofactor binding protein by using a wheat germ cell-free protein synthesis system coupled with unnatural amino acid probing" @default.
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• W2053196265 doi "https://doi.org/10.1002/prot.21341" @default.
• W2053196265 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17348022" @default.
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