Overview of Site-Selective Protein Editing By Backbone Extension Acyl
A post-translational backbone extension acyl rearrangement (BEAR) reaction has now been developed that converts a ribosomal protein product into a new product containing a β-peptide, γ-peptide ...
This strategy relies on an intramolecular backbone-extension acyl rearrangement (BEAR) reaction that post-translationally and site -specifically rearranges the backbone to introduce a new functional unit, in this case a β 2 -, ɣ-, or δ-linkage. This work involved contributions from the Chatterjee lab, Francis lab, Miller lab, and Schepartz lab.
Such details provide a deeper understanding and appreciation for Site Selective Protein Editing By Backbone Extension Acyl.
Introduction of such an α-hydroxy acid into a protein translated in vivo, followed by nucleophile unmasking, sets up a thermodynamically favored intramolecular backbone extension acyl rearrangement (BEAR) reaction that edits the protein to install an extended- backbone monomer.
Understanding Site Selective Protein Editing By Backbone Extension Acyl Before the Gallery
Site-selective editing of peptides via backbone modification - Organic. For Site Selective Protein Editing By Backbone Extension Acyl, this point helps readers notice the most relevant visual details before moving into the gallery.
DNA‐assisted site‐selective protein modification - PMC. It works as a short bridge between the article summary and the gallery section.
Contemporary approaches to site-selective protein modification | Nature. This note connects the source idea with the visuals in a simple, reader-friendly way.
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