Protein trans-splicing by split inteins holds great potential for the chemical modification and
semisynthesis of proteins. However, the structural requirements of the extein sequences …

We recently reported an artificially split intein based on the Ssp DnaB mini-intein that
consists of a synthetic N-terminal intein fragment (Int N) and a recombinant C-terminal part …

Inteins catalyze a protein splicing reaction to excise the intein from a precursor protein and
join the flanking sequences (exteins) with a peptide bond. In a split intein, the intein …

Protein trans-splicing mediated by a split intein reconstitutes a protein backbone from two
parts. This virtually traceless autoprocessive reaction provides the basis for numerous …

Inteins remove themselves from a precursor protein by protein splicing. Due to the
concomitant structural changes of the host protein, this self-processing reaction has enabled …

Inteins catalyze self‐excision from host precursor proteins while concomitantly ligating the
flanking substrates (exteins) with a peptide bond. Noncatalytic extein residues near the …

Protein trans-splicing by split inteins has many uses in protein production and research.
Splicing proteins with synthetic peptides, which employs atypical split inteins, is particularly …

Conventional split inteins have been useful for trans-splicing between recombinant proteins,
and an artificial S1 split intein is useful for adding synthetic peptide onto the N terminus of …

Protein splicing mediated by inteins is a self-processive reaction leading to the excision of
the internal intein domain from a precursor protein and the concomitant ligation of the …

Inteins are internal protein sequences that post-translationally self-excise and splice
together the flanking sequences, the so-called exteins. Natural and engineered inteins have …