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Issue 34, 2018
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Native chemical ligation at methionine bioisostere norleucine allows for N-terminal chemical protein ligation

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Abstract

The development of γ-thionorleucine (ThioNle) as a handle for native chemical ligation–desulfurization is reported here. ThioNle is a new addition to the expanding thiolated amino acid toolbox and serves as a methionine substitute in NCL with the advantage that it lacks the undesirable oxidation-prone thioether moiety. Its usefulness for N-terminal ubiquitination is demonstrated by efficient preparation of fully synthetic linear diubiquitin with preserved protein folding compared to the expressed material. Interestingly, gel-based deubiquitinating assays revealed that the methionine to norleucine substitution did affect diubiquitin cleavage, which may indicate a more profound role for methionine in the interaction between ubiquitin and the deubiquitinating enzymes than has been known so far.

Graphical abstract: Native chemical ligation at methionine bioisostere norleucine allows for N-terminal chemical protein ligation

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Publication details

The article was received on 10 Jul 2018, accepted on 09 Aug 2018 and first published on 09 Aug 2018


Article type: Paper
DOI: 10.1039/C8OB01627E
Citation: Org. Biomol. Chem., 2018,16, 6306-6315
  • Open access: Creative Commons BY-NC license
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    Native chemical ligation at methionine bioisostere norleucine allows for N-terminal chemical protein ligation

    B. Xin, B. D. M. van Tol, H. Ovaa and P. P. Geurink, Org. Biomol. Chem., 2018, 16, 6306
    DOI: 10.1039/C8OB01627E

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