Proteins constitute the majority of nature's worker biomolecules. Designed for specific
functions, complex tertiary structures make proteins ideal candidates for analysing natural …

Nature uses a limited, conservative set of amino acids to synthesize proteins. The ability to
genetically encode an expanded set of building blocks with new chemical and physical …

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 …

Protein lysine methylation is a distinct posttranslational modification that causes minimal
changes in the size and electrostatic status of lysine residues. Lysine methylation plays …

Chemists, biologists, and material scientists alike have long sought to control protein
presentation, orientation, and activity within biomaterials to dictate reaction catalysis …

Lysine (Lys) residues in proteins undergo a wide range of reversible post-translational
modifications (PTMs), which can regulate enzyme activities, chromatin structure, protein …

Over the past two decades, genetic code expansion (GCE)-enabled methods for
incorporating noncanonical amino acids (ncAAs) into proteins have significantly advanced …

Bioorthogonal phosphines were introduced in the context of the Staudinger ligation over 20
years ago. Since that time, phosphine probes have been used in myriad applications to tag …

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 …