Over the past 16 years, genetic code expansion and reprogramming in living organisms has
been transformed by advances that leverage the unique properties of pyrrolysyl-tRNA …

Virtually all natural proteins are built from only 20 amino acids, and while this makes
possible all the functions they perform, the ability to encode other amino acids selected for …

Expansion of the genetic code with nonstandard amino acids (nsAAs) has enabled
biosynthesis of proteins with diverse new chemistries. However, this technology has been …

The phosphorylation of threonine residues in proteins regulates diverse processes in
eukaryotic cells, and thousands of threonine phosphorylations have been identified. An …

The ability to selectively modify proteins at two or more defined locations opens new
avenues for manipulating, engineering, and studying living systems. As a chemical biology …

Adam W. Duster1, Hai Lin2. 1Integrative and Systems Biology, University of Colorado
Denver, Denver, CO, USA, 2Chemistry, University of Colorado Denver, Denver, CO, USA …

Photosynthetic organisms utilize dynamic and complex networks of pigments bound within
light-harvesting complexes to transfer solar energy from antenna complexes to reaction …

Various post-translational modifications can naturally occur on proteins, regulating the
activity, subcellular localization, interaction, or stability of the proteins. However, it can be …

Post‐translational modifications (PTMs) of proteins not only exponentially increase the
diversity of proteoforms, but also contribute to dynamically modulating the localization …

Pyrrolysyl-tRNA synthetase (PylRS) and its cognate tRNAPyl have emerged as ideal
translation components for genetic code innovation. Variants of the enzyme facilitate the …