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. 2015 Jun 25;5(3):1210–1227. doi: 10.3390/biom5031210

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© 2015 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).

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Chemical methods for the installation of ubiquitin and ubiquitin-like modifications. (a) Synthesis with δ-mercaptolysine. A synthetic peptide thioester containing a protected δ-mercaptolysine is reacted with a recombinant protein fragment to generate full-length α-synuclein. After deprotection of the δ-mercaptolysine residue, it can be selectively reacted with a recombinant ubiquitin thioester. Desulferization then gives site-specifically ubiquitination α-synuclein with no mutations. (b) Disulfide-directed ubiquitination. A C-terminal ubiquitin thiol, produced using intein chemistry, can be activated as a mixed disulfide, which can then be transferred to a cysteine residue on α-synuclein.