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C-GEM researchers developed a novel method called 3-Prime Adenosine-Retaining Aminoacyl–tRNA Isolation (PARTI), which determines precisely how much of a cellular tRNA is acylated, what it is acylated with, and whether it has been acylated once or twice. PARTI is an essential verification tool for optimizing… Read More »Breakthrough Article: Monitoring monomer-specific acyl–tRNA levels in cells with PARTI (Nucleic Acids Res, 2025)

C-GEM researchers developed a novel post-translational backbone editing reaction to replace a peptide bond with a C-C bond as diketones and heterocycles. This general strategy provides the first example of a C–C bond forming reaction to take place within the peptide backbone, as well as… Read More »Peptide Backbone Editing via Post-Translational O to C Acyl Shift (JACS, 2025)

C-GEM researchers found that a single atom change on tRNA—O to S on the 3′ terminal adenosine—does not hinder regular translation. Changing the 3’ oxo-ester on tRNA to a more reactive thioester had the potential to impact translation positively or negatively at multiple steps in… Read More »Thioesters Support Efficient Protein Biosynthesis by the Ribosome (ACS Cent Sci, 2025)

C-GEM researchers investigated whether preventing the binding of ribosomal protein bS1 could improve ribosome orthogonality. A current, common strategy for generating orthogonal ribosomes involves controlling mRNA and ribosome interactions by modifying the Shine-Dalgarno and anti-Shine-Dalgarno sequences, the sequence that sits upstream of the start codon… Read More »Role of Ribosomal Protein bS1 in Orthogonal mRNA Start Codon Selection (Biochemistry, 2025)