Protocol for protein modification using oxalyl thioester-mediated chemoselective ligation
Summary: 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 oxoSEA group, and...
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| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2024-12-01
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| Series: | STAR Protocols |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2666166724005550 |
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| Summary: | Summary: 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 oxoSEA 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.For complete details on the use and execution of this protocol, please refer to Snella et al.1 : Publisher’s note: Undertaking any experimental protocol requires adherence to local institutional guidelines for laboratory safety and ethics. |
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| ISSN: | 2666-1667 |