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

被引：47

作者：

Berrade, Luis ^{[1
]}

Camarero, Julio A. ^{[1
]}

机构：

[1] Univ So Calif, Sch Pharm, Dept Pharmacol & Pharmaceut Sci, Los Angeles, CA 90033 USA

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2009年 / 66卷 / 24期

关键词：

Chemical ligation; Protein alpha-thioesters; Intein; Protein splicing; Circular polypeptides; Post-translational modifications; Isotopic labeling; NATIVE CHEMICAL LIGATION; TGF-BETA RECEPTOR; SITE-SPECIFIC IMMOBILIZATION; FMOC-BASED SYNTHESIS; N-TERMINAL CYSTEINE; RECOMBINANT PROTEINS; SPLICING ELEMENT; UNPROTECTED PEPTIDES; MACROCYCLIC PEPTIDES; KINASE ACTIVATION;

D O I：

10.1007/s00018-009-0122-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：3909 / 3922

页数：14

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