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A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer.


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.

SUBMITTER: Brustad EM 

PROVIDER: S-EPMC2743202 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

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A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer.

Brustad Eric M EM   Lemke Edward A EA   Schultz Peter G PG   Deniz Ashok A AA  

Journal of the American Chemical Society 20081201 52


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  ...[more]

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