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A General and Efficient Method for the Site-Specific Dual-Labeling of Proteins for Single Molecule Fluorescence Resonance Energy Transfer

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Brustad, Eric M., Lemke, Edward A., Schultz, Peter G., Deniz, Ashok A.·2008·Journal of the American Chemical Society

Abstract

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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Metadata

Authors
Brustad, E. M., Lemke, E. A., Schultz, P. G., & Deniz, A. A.
Venue
Journal of the American Chemical Society
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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