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

Authors :: Wei T
Liu H
Wu H
Pu F
Li X
Source :: STAR protocols [STAR Protoc] 2021 Aug 25; Vol. 2 (3), pp. 100777. Date of Electronic Publication: 2021 Aug 25 (Print Publication: 2021).
Publication Year :: 2021
Abstract: 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).<br />Competing Interests: The authors declare no competing interests.<br /> (© 2021 The Author(s).)

Subjects :: Phosphorylation
Serine chemistry
Serine metabolism
Threonine chemistry
Threonine metabolism
HMGA1a Protein chemical synthesis
HMGA1a Protein chemistry
HMGA1a Protein metabolism
Protein Processing, Post-Translational
Recombinant Proteins chemical synthesis
Recombinant Proteins chemistry
Recombinant Proteins metabolism
Solid-Phase Synthesis Techniques methods

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