Protocol for protein modification using oxalyl thioester-mediated chemoselective ligation
Résumé
Protocol for protein modification using oxalyl thioester-mediated chemoselective ligation
The development of fast ligation chemistries for the site-specific modification of proteins has become a major focus in chemical biology. We describe steps for preparing an oxalyl thioester precursor in the form of an N-oxalyl perhydro-1,2,5-dithiazepine handle, i.e., the oxo SEA group, and incorporating it into a peptide modifier using solid phase peptide synthesis. We then detail procedures for its application for the modification of an N-terminal Cys-containing B1 domain of the streptococcal G protein using the native chemical ligation.
Domaines
Chimie| Origine | Fichiers éditeurs autorisés sur une archive ouverte |
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