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

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 introduce...

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Detalles Bibliográficos
Autores principales: Wei, Tongyao, Liu, Heng, Wu, Hongxiang, Pu, Fan, Li, Xuechen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2021
Materias:
Protocol
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8406030/
https://www.ncbi.nlm.nih.gov/pubmed/34485943
http://dx.doi.org/10.1016/j.xpro.2021.100777
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author Wei, Tongyao
Liu, Heng
Wu, Hongxiang
Pu, Fan
Li, Xuechen
author_facet Wei, Tongyao
Liu, Heng
Wu, Hongxiang
Pu, Fan
Li, Xuechen
author_sort Wei, Tongyao
collection PubMed
description 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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spelling pubmed-84060302021-09-02 Serine/threonine ligation-assisted chemical synthesis of HMGA1a protein with site-specific post-translational modifications Wei, Tongyao Liu, Heng Wu, Hongxiang Pu, Fan Li, Xuechen STAR Protoc Protocol 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). Elsevier 2021-08-25 /pmc/articles/PMC8406030/ /pubmed/34485943 http://dx.doi.org/10.1016/j.xpro.2021.100777 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Protocol
Wei, Tongyao
Liu, Heng
Wu, Hongxiang
Pu, Fan
Li, Xuechen
Serine/threonine ligation-assisted chemical synthesis of HMGA1a protein with site-specific post-translational modifications
title Serine/threonine ligation-assisted chemical synthesis of HMGA1a protein with site-specific post-translational modifications
title_full Serine/threonine ligation-assisted chemical synthesis of HMGA1a protein with site-specific post-translational modifications
title_fullStr Serine/threonine ligation-assisted chemical synthesis of HMGA1a protein with site-specific post-translational modifications
title_full_unstemmed Serine/threonine ligation-assisted chemical synthesis of HMGA1a protein with site-specific post-translational modifications
title_short Serine/threonine ligation-assisted chemical synthesis of HMGA1a protein with site-specific post-translational modifications
title_sort serine/threonine ligation-assisted chemical synthesis of hmga1a protein with site-specific post-translational modifications
topic Protocol
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8406030/
https://www.ncbi.nlm.nih.gov/pubmed/34485943
http://dx.doi.org/10.1016/j.xpro.2021.100777
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