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- W4237996149 abstract "Inteins are naturally occurring proteins that are involved in the precise cleavage and formation of peptide bonds in a process known as protein splicing. Genetic engineering has allowed the controllable cleavage of peptide bonds at either the N- or C-terminus of the intein. Inteins displaying controllable cleavage have been used in the isolation of bacterially expressed proteins possessing either a C-terminal thioester or an N-terminal cysteine. The specific placement of these reactive groups has allowed either protein–protein or protein–peptide condensation through a native peptide bond. This review describes the methods used to specifically generate these reactive groups on bacterially expressed proteins and some applications of this technique, known as intein-mediated protein ligation. Furthermore, a versatile two intein (TWIN) system will be described which enables the circularization and polymerization of bacterially expressed proteins or peptides. © 2000 John Wiley & Sons, Inc. Biopoly 51: 333–342, 1999" @default.
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- W4237996149 date "1999-01-01" @default.
- W4237996149 modified "2023-09-26" @default.
- W4237996149 title "Intein-mediated protein ligation: Harnessing nature's escape artists" @default.
- W4237996149 doi "https://doi.org/10.1002/(sici)1097-0282(1999)51:5<333::aid-bip3>3.3.co;2-r" @default.
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