A Pyrrolysine Analogue for Site‐Specific Protein Ubiquitination | Zendy

Li Xin | Zendy; Fekner Tomasz | Zendy; Ottesen Jennifer J. | Zendy; Chan Michael K. | Zendy

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A Pyrrolysine Analogue for Site‐Specific Protein Ubiquitination

Author(s) -

Li Xin,

Fekner Tomasz,

Ottesen Jennifer J.,

Chan Michael K.

Publication year - 2009

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.200904472

Subject(s) - ubiquitin , residue (chemistry) , lysine , native chemical ligation , polypeptide chain , chemistry , side chain , stereochemistry , biochemistry , computational biology , amino acid , biology , chemical synthesis , in vitro , organic chemistry , gene , polymer

The art of stitching proteins : D ‐Cys‐ε‐Lys and its diastereomer L ‐Cys‐ε‐Lys read through the UAG codon (see scheme). As the resulting proteins can participate in native chemical ligation (NCL), this process provides a means to prepare proteins chemoselectively modified (e.g. ubiquitinated) through a peptidic side chain located at the ε position of a rationally selected lysine residue.

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