Chemical Synthesis of HMGA1a Proteins with Post-translational Modifications via Ser/Thr Ligation


The first chemical synthesis of nuclear protein HMGA1a via Ser/Thr ligation is reported. Notably, Hmb (2-<u>h</u>ydroxy-4-<u>m</u>ethoxy<u>b</u>enzyl) exhibits crucial improvement of both the difficult coupling during solid phase peptide synthesis and the poor ligation encountered in protein synthesis. These efforts led to preparation of HMGA1a analogs with well-defined phosphorylation and methylation patterns (9 synthetic proteins in total), thus overcoming the heterogeneous and combinatory problems inherent to protein <u>p</u>ost-<u>t</u>ranslational <u>m</u>odifications (PTMs), and facilitating the study of the regulatory roles of such PTMs

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oai:figshare.com:article/4210089Last time updated on 2/12/2018

This paper was published in FigShare.

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