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A General and Efficient Method for the Site-Specific Dual-Labeling of Proteins for Single Molecule Fluorescence Resonance Energy Transfer
Open accessAbstract
A general strategy for the site-specific dual-labeling of proteins for single-molecule fluorescence resonance energy transfer is presented. A genetically encoded unnatural ketone amino acid was labeled with a hydroxylamine-containing fluorophore with high yield (>95%) and specificity. This methodology was used to construct dual-labeled T4 lysozyme variants, allowing the study of T4 lysozyme folding at single-molecule resolution. The presented strategy is anticipated to expand the scope of single-molecule protein structure and function studies.
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Young, T. S., & Schultz, P. G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.091306 · Cited by 354
Self-citationChen, Z., Chen, M., Cheng, Y., Kowada, T., Xie, J., Zheng, X., & Rao, J. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.201913314 · Cited by 71
Metadata
- Authors
- Brustad, E. M., Lemke, E. A., Schultz, P. G., & Deniz, A. A.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-12-09
- Volume
- 130
- Issue
- 52
- Pages
- 17664-17665
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2015442731
- Cited by
- 185
- References
- 0
- FWCI
- 6.06
- Type
- journal article
- Language
- en
- Open access
- green
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- Brustad, E. M., Lemke, E. A., Schultz, P. G., & Deniz, A. A. (2008). A General and Efficient Method for the Site-Specific Dual-Labeling of Proteins for Single Molecule Fluorescence Resonance Energy Transfer. Journal of the American Chemical Society. https://doi.org/10.1021/ja807430h
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