ArticleNature chemical biology2020
Multiplexed genomic encoding of non-canonical amino acids for labeling large complexes.
Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Site-Specific Protein Bioconjugation Through Cellular Incorporation of Noncanonical Amino Acids.Angewandte Chemie (International ed. in English) · 2026Review
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Comparing FRET Pairs that Report on Intersubunit Rotation in Bacterial Ribosomes.Journal of molecular biology · 2023Article
- Comparing FRET pairs that report on intersubunit rotation in bacterial ribosomes.bioRxiv : the preprint server for biology · 2023Article
- The Structural Dynamics of Translation.Annual review of biochemistry · 2022Review
- Insights into genome recoding from the mechanism of a classic +1-frameshifting tRNA.Nature communications · 2021Article
- Mechanistic studies of non-canonical amino acid mutagenesis.Methods in enzymology · 2021Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Stunning advances in the structural biology of multicomponent biomolecular complexes (MBCs) have ushered in an era of intense, structure-guided mechanistic and functional studies of these complexes. Nonetheless, existing methods to site-specifically conjugate MBCs with biochemical and biophysical labels are notoriously impracticable and/or significantly perturb MBC assembly and function. To overcome these limitations, we have developed a general, multiplexed method in which we genomically encode non-canonical amino acids (ncAAs) into multiple, structure-informed, individual sites within a target MBC; select for ncAA-containing MBC variants that assemble and function like the wildtype MBC; and site-specifically conjugate biochemical or biophysical labels to these ncAAs. As a proof-of-principle, we have used this method to generate unique single-molecule fluorescence resonance energy transfer (smFRET) signals reporting on ribosome structural dynamics that have thus far remained inaccessible to smFRET studies of translation.
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