AI Article Synopsis
- The study shows how a specific chemical modification can be added and removed from proteins, allowing for better visualization and manipulation of these proteins.
- Researchers focus on a process involving a protein from E. coli called acyl carrier protein, using a technique for post-translational modification.
- The method allows them to label different versions of this protein for in-depth analysis using NMR, highlighting how proteins interact with their substrates.
Article Abstract
The reversible covalent attachment of chemical probes to proteins has long been sought as a means to visualize and manipulate proteins. Here we demonstrate the full reversibility of post-translational custom pantetheine modification of Escherichia coli acyl carrier protein for visualization and functional studies. We use this iterative enzymatic methodology in vitro to reversibly label acyl carrier protein variants and apply these tools to NMR structural studies of protein-substrate interactions.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4128096 | PMC |
| http://dx.doi.org/10.1038/nmeth.2175 | DOI Listing |
Publication Analysis
Top Keywords
acyl carrier
8
carrier protein
8
reversible labeling
4
labeling native
4
native fusion-protein
4
fusion-protein motifs
4
motifs reversible
4
reversible covalent
4
covalent attachment
4
attachment chemical
4
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!