We have located links that may give you full text access.
Site-specific reversible protein and peptide modification: transglutaminase-catalyzed glutamine conjugation and bioorthogonal light-mediated removal.
Bioconjugate Chemistry 2019 April 5
Dynamic photoswitches in proteins that impart spatial and temporal control are important to manipulate and study biotic and abiotic processes. Nonetheless, approaches to install these switches into proteins site-specifically are limited. Herein we describe a novel site-specific method to generate photo-removable protein conjugates. Amine-containing chromophores (e.g., venerable o-nitrobenzyl and less-explored o-nitrophenylethyl groups) were incorporated via transamidation into glutamine side-chain of alpha-gliadin, LCMV and TAT peptides, as well as beta-casein and UmuD proteins by transglutaminase (TGase, EC 2.3.2.13). Subsequently, photolysis regenerated the native peptides and proteins. When this modification leads to the reduction or abolishment of certain activities, the process is referred to as caging, as in the case for E. coli polymerase manager protein UmuD. Importantly, this method is simple, robust and easily adaptable, e.g., all components are commercially available.
Full text links
Related Resources
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app