Introduction

Inteins are internal protein segments embedded in various host proteins and are excised by a post-translational process called protein splicing (Perler et al. 1994). During protein splicing, the intein catalyzes the precise cleavage of peptide bonds at its termini and ligation of its flanking protein sequences (termed exteins) without the need for any exogenous factors (Paulus 2000). Characterization of key catalytic residues in the protein-splicing pathway has led to a number of novel strategies for protein research. This chapter is dedicated to a brief review of various intein-related applications in protein purification, and protein/peptide ligation. In particular, we introduce some new approaches in protein manipulation and characterization such as protein trans-cleavage, kinase assays, and peptide arrays.

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