期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 66, 期 24, 页码 3909-3922出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-009-0122-3
关键词
Chemical ligation; Protein alpha-thioesters; Intein; Protein splicing; Circular polypeptides; Post-translational modifications; Isotopic labeling
资金
- NIGMS NIH HHS [R01 GM090323] Funding Source: Medline
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.
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