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Serine/threonine ligation-assisted chemical synthesis of HMGA1a protein with site-specific post-translational modifications.

STAR protocols (2021-09-07)
Tongyao Wei, Heng Liu, Hongxiang Wu, Fan Pu, Xuechen Li
RÉSUMÉ

Dissecting the function of proteins' post-translational modifications (PTMs) is seriously hindered by the difficulty in obtaining the homogeneous protein with the PTMs of interest. Chemical protein synthesis offers a great potential to overcome this limitation. Here, a detailed protocol is introduced for chemical synthesis of HMGA1a protein with site-specific modifications via Ser/Thr ligation strategy, by which we can systematically study the function of the triple phosphorylation (3pSer) in the HMGA1a acidic tail. For complete details on the use and execution of this protocol, please refer to Wei et al. (2021).

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Sigma-Aldrich
Glycérol, for molecular biology, ≥99.0%
Sigma-Aldrich
Chlorure de sodium, for molecular biology, DNase, RNase, and protease, none detected, ≥99% (titration)
Sigma-Aldrich
Diethylamine, ≥99.5%