Mechanistic studies of non-canonical amino acid mutagenesis
Fleisher, R. C.; Michael, N.; Gonzalez, R. L.
Show abstract
Over the past decade, harnessing the cellular protein synthesis machinery to incorporate non-canonical amino acids (ncAAs) into tailor-made peptides has significantly advanced many aspects of molecular science. More recently, groundbreaking progress in our ability to engineer this machinery for improved ncAA incorporation has led to significant enhancements of this powerful tool for biology and chemistry. By revealing the molecular basis for the poor or improved incorporation of ncAAs, mechanistic studies of ncAA incorporation by the protein synthesis machinery have tremendous potential for informing and directing such engineering efforts. In this chapter, we describe a set of complementary biochemical and single-molecule fluorescence assays that we have adapted for mechanistic studies of ncAA incorporation. Collectively, these assays provide data that can guide engineering of the protein synthesis machinery to expand the range of ncAAs that can be incorporated into peptides and increase the efficiency with which they can be incorporated, thereby enabling the full potential of ncAA mutagenesis technology to be realized.
Matching journals
The top 2 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Synthesis of modified nucleotide polymers by the poly(U) polymerase Cid1: Application to direct RNA sequencing on nanopores. 95%
- Safe and easy evaluation of tmRNA-SmpB-mediated trans-translation in ESKAPE pathogenic bacteria 95%
- Development, validation, and application of the ribosome separation and reconstitution system for protein translation in vitro 94%
Similar papers in this journal
- Fuzzy RNA-recognition by the Trypanosoma brucei editosome 94%
- Base composition at the start of the coding sequence controls the balance between translation initiation and mRNA degradation in E. coli . 94%
- Coordination of -1 Programmed Ribosomal Frameshifting by Transcript and Nascent Chain Features Revealed by Deep Mutational Scanning 94%
Similar papers in this journal
Similar papers in this journal
- A real-time biochemical assay for quantitative analyses of APOBEC-catalyzed DNA deamination 93%
- tRNA m1G9 modification depends on substrate-specific RNA conformational changes induced by the methyltransferase Trm10 92%
- BR-Bodies Facilitate Adaptive Responses and Survival During Copper Stress in Caulobacter crescentus 92%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.