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• W2046165093 abstract "The combination of a genetically encoded aldehyde tag and optimized labeling method allows high-efficiency, site-specific labeling of tagged proteins after purification or in cell extracts. The authors use the high labeling efficiency for single-molecule measurements of the dynamic interactions between two DNA polymerases and polymerase processivity factor bound to DNA. A major hurdle for molecular mechanistic studies of many proteins is the lack of a general method for fluorescence labeling with high efficiency, specificity and speed. By incorporating an aldehyde motif genetically into a protein and improving the labeling kinetics substantially under mild conditions, we achieved fast, site-specific labeling of a protein with ∼100% efficiency while maintaining the biological function. We show that an aldehyde-tagged protein can be specifically labeled in cell extracts without protein purification and then can be used in single-molecule pull-down analysis. We also show the unique power of our method in single-molecule studies on the transient interactions and switching between two quantitatively labeled DNA polymerases on their processivity factor." @default.
• W2046165093 created "2016-06-24" @default.
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• W2046165093 date "2012-04-01" @default.
• W2046165093 modified "2023-10-18" @default.
• W2046165093 title "Quantitative fluorescence labeling of aldehyde-tagged proteins for single-molecule imaging" @default.
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• W2046165093 doi "https://doi.org/10.1038/nmeth.1954" @default.
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