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• W2955755781 startingPage "12599" @default.
• W2955755781 abstract "Abstract α‐Ketoacid‐hydroxylamine (KAHA) ligation allows the coupling of unprotected peptide segments through the chemoselective formation of an amide bond. Currently, the most widely used variant employs a 5‐membered cyclic hydroxylamine that forms a homoserine ester as the primary ligation product. In order to directly form amide‐linked threonine residues at the ligation site, we prepared a new 4‐membered cyclic hydroxylamine building block. This monomer was applied to the synthesis of wild‐type ubiquitin‐conjugating enzyme UbcH5a (146 residues) and Titin protein domain TI I27 (89 residues). Both the resulting UbcH5a and the variant with two homoserine residues showed identical activity to a recombinant variant in a ubiquitination assay." @default.
• W2955755781 created "2019-07-12" @default.
• W2955755781 creator A5008775174 @default.
• W2955755781 creator A5021952863 @default.
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• W2955755781 date "2019-07-24" @default.
• W2955755781 modified "2023-10-02" @default.
• W2955755781 title "A Threonine‐Forming Oxazetidine Amino Acid for the Chemical Synthesis of Proteins through KAHA Ligation" @default.
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• W2955755781 doi "https://doi.org/10.1002/anie.201906486" @default.
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