The native chemical ligation reaction (NCL) involves reacting a C-terminal peptide thioester
with an N-terminal cysteinyl peptide to produce a native peptide bond between the two …

The growing interest in proteins, both in fundamental research and in drug discovery, has
fuelled demand for efficient synthetic methods to access these biomolecules. Although solid …

Despite the great promise of genetic code expansion technology to modulate structures and
functions of proteins, external addition of ncAAs is required in most cases and it often limits …

Nature has developed a plethora of protein machinery to operate and maintain nearly every
task of cellular life. These processes are tightly regulated via post‐expression modifications …

Sulfonation as one of the most important modification reactions in nature is essential for
many biological macromolecules to function. Development of green sulfonate group donor …

Tyrosine sulfation is a common posttranslational modification in mammals. To date, it has
been thought to be limited to secreted and transmembrane proteins, but little is known about …

Saliva of ticks is arguably the most complex saliva of any animal. This is particularly the case
for ixodid species that feed for many days firmly attached to the same skin site of their …

Thrombin is the key enzyme of the entire hemostatic process since it is able to exert both
procoagulant and anticoagulant functions; therefore, it represents an attractive target for the …

Native chemical ligation (NCL) provides a powerful solution to assemble proteins with
precise chemical features, which enables a detailed investigation of the protein structure …

Tyrosine sulfation is an important post-translational modification found in higher eukaryotes.
Here we report an engineered tyrosyl-tRNA synthetase/tRNA pair that co-translationally …