Ontology highlight
ABSTRACT:
SUBMITTER: Brustad EM
PROVIDER: S-EPMC2743202 | biostudies-literature | 2008 Dec
REPOSITORIES: biostudies-literature
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]