Chemical synthesis is the most powerful way to assemble selectively modified proteins and
is a tool for engineering proteins that are inaccessible by standard site-directed …

Expression of recombinant proteins as fusions with SUMO (s mall u biquitin‐related m
odifier) protein has significantly increased the yield of difficult‐to‐express proteins in …

Here, we describe an Se-auxiliary mediated ligation protocol capable of rapid native
chemical ligations at sterically hindered junctions, followed by in situ auxiliary cleavage …

Chimeric proteins, including bispecific antibodies, are biological tools with therapeutic
applications. Genetic fusion and ligation methods allow the creation of N-to-C and C-to-N …

We describe a prokaryotic expression system using the autoproteolytic function of Npro from
classical swine fever virus. Proteins or peptides expressed as Npro fusions are deposited as …

Engineered protein tags that confer specific binding to standardized affinity resins have
revolutionized recombinant protein purification. Ideally, these tags should, however, be …

The native chemical ligation reaction has been used extensively for the synthesis of the
large polypeptides that correspond to folded proteins and domains. The efficiency of the …

The selective coupling of unprotected peptide fragments is an essential element of many
approaches for the total and semisynthesis of proteins. 1 This coupling can be achieved …

Sequence–specific enzymatic cleavage of protein fusions is an important application in
recombinant protein technology. We have used the Neisseria type 2 lgA protease (EC 3.4 …

A single point mutation has been engineered in the tyrosyl-tRNA synthetase that improves
its affinity (KM) for its substrate ATP by a factor of 100. In the crystal structure of the tyrosyl …