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

Tongyao Wei; Heng Liu; Hongxiang Wu; Fan Pu; Xuechen Li

STAR Protocols (Sep 2021)

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

Tongyao Wei,
Heng Liu,
Hongxiang Wu,
Fan Pu,
Xuechen Li

Affiliations

Tongyao Wei: Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong, Hong Kong, P.R. China; Corresponding author
Heng Liu: Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong, Hong Kong, P.R. China
Hongxiang Wu: Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong, Hong Kong, P.R. China
Fan Pu: Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong, Hong Kong, P.R. China
Xuechen Li: Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong, Hong Kong, P.R. China; Corresponding author

Journal volume & issue: Vol. 2, no. 3
p. 100777

Abstract

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Summary: 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).

Published in STAR Protocols

ISSN: 2666-1667 (Online)
Publisher: Elsevier
Country of publisher: United States
LCC subjects: Science: Science (General)
Website: https://star-protocols.cell.com/

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