Fast Protein Modification in the Nanomolar ...
Document type :
Compte-rendu et recension critique d'ouvrage
DOI :
PMID :
Title :
Fast Protein Modification in the Nanomolar Concentration Range Using an Oxalyl Amide as Latent Thioester**
Author(s) :
Snella, Benoît [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Grain, Benjamin [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Vicogne, Jérôme [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Capet, Frédéric [Auteur]
Unité de Catalyse et Chimie du Solide - UMR 8181 [UCCS]
Wiltschi, Birgit [Auteur]
Universität für Bodenkultur Wien = University of Natural Resources and Life Sciences [Vienne, Autriche] [BOKU]
Melnyk, Oleg [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Agouridas, Vangelis [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Centrale Lille
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Grain, Benjamin [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Vicogne, Jérôme [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Capet, Frédéric [Auteur]
Unité de Catalyse et Chimie du Solide - UMR 8181 [UCCS]
Wiltschi, Birgit [Auteur]
Universität für Bodenkultur Wien = University of Natural Resources and Life Sciences [Vienne, Autriche] [BOKU]
Melnyk, Oleg [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Agouridas, Vangelis [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Centrale Lille
Journal title :
Angewandte Chemie International Edition
Pages :
e202204992
Publisher :
Wiley-VCH Verlag
Publication date :
2022-07-18
ISSN :
1433-7851
English keyword(s) :
Latency
N
S-Acyl Shift Systems
Non-Native Ligation
Protein Modification
Thioester
N
S-Acyl Shift Systems
Non-Native Ligation
Protein Modification
Thioester
HAL domain(s) :
Chimie/Chimie organique
French abstract :
We show that latent oxalyl thioester surrogates are a powerful means to modify peptides and proteins in highly dilute conditions in purified aqueous media or in mixtures as complex as cell lysates. Designed to be shelf-stable ...
Show more >We show that latent oxalyl thioester surrogates are a powerful means to modify peptides and proteins in highly dilute conditions in purified aqueous media or in mixtures as complex as cell lysates. Designed to be shelf-stable reagents, they can be activated on demand to enable ligation reactions with peptide concentrations as low as a few hundred nM at rates approaching 30 M-1 s-1 .Show less >
Show more >We show that latent oxalyl thioester surrogates are a powerful means to modify peptides and proteins in highly dilute conditions in purified aqueous media or in mixtures as complex as cell lysates. Designed to be shelf-stable reagents, they can be activated on demand to enable ligation reactions with peptide concentrations as low as a few hundred nM at rates approaching 30 M-1 s-1 .Show less >
Language :
Français
Popular science :
Non
Source :
Files
- https://hal.archives-ouvertes.fr/hal-03838475/document
- Open access
- Access the document
- https://hal.archives-ouvertes.fr/hal-03838475/document
- Open access
- Access the document
- Snella-2022-Fast-protein-modification-in-the-na.pdf
- Open access
- Access the document
- document
- Open access
- Access the document