Split-protein systems have emerged as a powerful tool for detecting biomolecular
interactions and reporting biological reactions. However, reliable methods for identifying …

Protein splicing domains, also called inteins, have become a powerful biotechnological tool
for applications involving molecular biology and protein engineering. Early applications of …

Split inteins are parasitic genetic elements frequently found inserted into reading frames of
essential proteins. Their association and excision restore host protein function through a …

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 …

Expressed protein ligation is a simple and powerful method in protein engineering to
introduce sequences of unnatural amino acids, posttranslational modifications, and …

Protein splicing is a self‐catalyzed process in which an internal protein domain (the intein) is
excised from its flanking sequences, linking them together with a canonical peptide bond …

Protein trans-splicing (PTS) by split inteins has found widespread use in chemical biology
and biotechnology. Herein, we describe the use of a consensus design approach to …

Naturally split inteins have found widespread use in chemical biology due to their ability to
drive the ligation of separately expressed polypeptides through a process termed protein …

Split-inteins are a subset of inteins that are expressed in two separate halves and catalyze
splicing in trans upon association of the two domains. They occur naturally and have also …

Inteins are unique single-turnover enzymes that can excise themselves from the precursor
protein without the aid of any external cofactors or energy. In most cases, inteins are …