Over 500 natural and synthetic amino acids have been genetically encoded in the last two
decades. Incorporating these noncanonical amino acids into proteins enables many …

Since the establishment of site-specific mutagenesis of single amino acids to interrogate
protein function in the 1970s, biochemists have sought to tailor protein structure in the native …

The study of biomolecules in their native environments is a challenging task because of the
vast complexity of cellular systems. Technologies developed in the last few years for the …

The past two decades have witnessed the emergence of macrocycles, including macrocyclic
peptides, as a promising yet underexploited class of de novo drug candidates. Both …

A unique transfer RNA (tRNA)/aminoacyl-tRNA synthetase pair has been generated that
expands the number of genetically encoded amino acids in Escherichia coli. When …

Fluorescence spectroscopy, one of the most informative and sensitive analytical techniques,
has played and continues to play key roles in modern research. Indeed, unraveling the inner …

Recently, a general method was developed that makes it possible to genetically encode
unnatural amino acids with diverse physical, chemical, or biological properties in …

Although chemists can synthesize virtually any small organic molecule, our ability to
rationally manipulate the structures of proteins is quite limited, despite their involvement in …

▪ Abstract Expressed protein ligation (EPL) is a protein engineering approach that allows
recombinant and synthetic polypeptides to be chemoselectively and regioselectively joined …

Here we describe a de novo tRNA acylation system, the flexizyme (Fx) system, for the
preparation of acyl tRNAs with nearly unlimited selection of amino and hydroxy acids and …