Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 130, Issue 52, Pages 17664-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja807430h
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Funding
- U.S. Department of Energy, Division of Materials Sciences [DE-FG03-00HR46051]
- NIH [GM066833]
- AvH fellowship
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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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