Cellular and Molecular Life Sciences

, 66:3909

Expressed protein ligation: a resourceful tool to study protein structure and function

Review

DOI: 10.1007/s00018-009-0122-3

Cite this article as:
Berrade, L. & Camarero, J.A. Cell. Mol. Life Sci. (2009) 66: 3909. doi:10.1007/s00018-009-0122-3

Abstract

This review outlines the use of expressed protein ligation (EPL) to study protein structure, function and stability. EPL is a chemoselective ligation method that allows the selective ligation of unprotected polypeptides from synthetic and recombinant origin for the production of semi-synthetic protein samples of well-defined and homogeneous chemical composition. This method has been extensively used for the site-specific introduction of biophysical probes, unnatural amino acids, and increasingly complex post-translational modifications. Since it was introduced 10 years ago, EPL applications have grown increasingly more sophisticated in order to address even more complex biological questions. In this review, we highlight how this powerful technology combined with standard biochemical analysis techniques has been used to improve our ability to understand protein structure and function.

Keywords

Chemical ligationProtein α-thioestersInteinProtein splicingCircular polypeptidesPost-translational modificationsIsotopic labeling

Copyright information

© Birkhäuser Verlag, Basel/Switzerland 2009

Authors and Affiliations

  1. 1.Department of Pharmacology and Pharmaceutical Sciences, School of PharmacyUniversity of Southern CaliforniaLos AngelesUSA