ArticleACS chemical biology2009
A general method for scanning unnatural amino acid mutagenesis.
Article in ACS chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Directed evolution of the fluorescent protein CGP withApplied and environmental microbiology · 2024Article
- Accessing unexplored regions of sequence space in directed enzyme evolution via insertion/deletion mutagenesis.Nature communications · 2020Article
- Biogenesis, quality control, and structural dynamics of proteins as explored in living cells via site-directed photocrosslinking.Protein science : a publication of the Protein Society · 2019Review
- Article
- Structural plasticity of green fluorescent protein to amino acid deletions and fluorescence rescue by folding-enhancing mutations.BMC biochemistry · 2015Article
- Exploring the potential impact of an expanded genetic code on protein function.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Directed evolution of GFP with non-natural amino acids identifies residues for augmenting and photoswitching fluorescence.Chemical science · 2015Article
- Article
- A transposase strategy for creating libraries of circularly permuted proteins.Nucleic acids research · 2012Article
- A method for multi-codon scanning mutagenesis of proteins based on asymmetric transposons.Protein engineering, design & selection : PEDS · 2012Article
- Random mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G.PloS one · 2012Article
- Experimental methods for scanning unnatural amino acid mutagenesis.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Synthetic approach to stop-codon scanning mutagenesis.Journal of the American Chemical Society · 2011Article
- Optimizing non-natural protein function with directed evolution.Current opinion in chemical biology · 2011Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Current approaches to protein site-directed mutagenesis require an independent user operation for each mutation. This can impede large-scale scanning mutagenesis projects such as the mapping of protein interaction surfaces, active sites, or epitopes. It also prevents the creation of protein libraries of defined complexity for directed evolution purposes. Here we present a simple, fast, and effective way to perform scanning codon mutagenesis throughout a protein sequence. The process allows the researcher to define the new codon change, and therefore any amino acid mutation can be achieved. We demonstrate this approach by creating a library of proteins that contain single unnatural amino acid mutations encoded by the amber stop codon, TAG. The mutant proteins generated by this method can be expressed and assayed individually or used together as a mixed population of "rationally diversified" protein sequences.
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Registered trials
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