A recent study by Ruben L. Gonzalez Jr. and coworkers provides insight into how to improve the incorporation of D-α-amino acids into proteins.

By Patrick Ginther In a recent 2018 Nature news & views, the work of Jason Chin and co-workers was highlighted for the lab’s extraordinary work on developing new tools for synthetic biology [1]. Specifically, Chin and co-workers successfully generated a variant of the pyrrolysyl-tRNA synthetase/tRNA… Read More »Driving orthogonality between variant pyrrolysyl-tRNA synthetase/tRNA pairs

Riboswitches are defined as RNA structures, typically found in the 5’ untranslated region (5’UTR) of mRNA, that sense and respond to small molecules, metabolites, or coenzymes to regulate transcription and translation.

Ribosome assembly is a remarkably complex cellular process. In the yeast large subunit (60S) alone, it requires the ordered association and folding of 3 rRNAs and 46 r-proteins as the nascent ribosomes move from the nucleolus, to the nucleus, and finally to the cytoplasm.

In a recent paper in JACS, Schultz and co-workers present a strategy where replacing a key amino acid of an enzyme by a non-standard amino acid (nsAA) produces an organism that requires this nsAA for survival. ..

Posttranslational modifications (PTMs) are responsible for some of the most exotic ribosomally synthesized peptide backbones in biology.

the most recent issue of Organic and Biomolecular Chemistry, a paper from Matthew Hartman’s lab highlights the use of an editing-deficient valine-tRNA synthetase (ValRS T222P) to incorporate 11 non-canonical amino acids (ncAAs) into peptides synthesized in vitro.