In protein trans-splicing, an intein domain split into two polypeptide chains mediates linkage
of the flanking amino acid sequences, the N-and C-terminal exteins, with a native peptide …

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 …

Background Protein trans-splicing by naturally occurring split DnaE inteins is used for
protein ligation of foreign peptide fragments. In order to widen biotechnological applications …

Split inteins play an important role in modern protein semisynthesis techniques. These
naturally occurring protein splicing domains can be used for in vitro and in vivo protein …

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 …

A naturally occurring trans-splicing intein from the dnaE gene of Synechocystis sp.
PCC6803 (Ssp DnaE intein) was used to characterize the intein-catalyzed splicing reaction …

A 429 aa theoretical intein is encoded in the dnaB gene (DNA helicase) of the
cyanobacterium Synechocystis sp. strain PCC6803. This intein is shown to be capable of …

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 …

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 …

Split inteins carry out a naturally occurring process known as protein trans‐splicing, where
two protein fragments bind to form a catalytically competent enzyme, then catalyze their own …