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Updated: Feb 10, 2026
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Bioorthogonal Chemical Imaging of Cell Metabolism Regulated by Aromatic Amino Acids
Published on: May 12, 2023
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Late metabolic precursors for selective aromatic residue labeling
Julia Schörghuber1, Leonhard Geist2, Gerald Platzer2
1Institute of Organic Chemistry, University of Vienna, Währinger Str. 38, 1090, Vienna, Austria.
Journal of Biomolecular NMR
|May 30, 2018
Summary
We developed cost-effective heavy isotope precursors for E. coli protein production. These tools enhance protein NMR spectroscopy for drug development by enabling precise labeling for structural and interaction studies.
Area of Science:
- Biochemistry
- Structural Biology
- Drug Development
Background:
- Protein NMR spectroscopy is crucial for drug development.
- High costs and technical challenges limit its routine application.
- Efficient methods for producing isotopically labeled proteins are needed.
Purpose of the Study:
- To present a toolbox of heavy isotope-containing amino acid precursors.
- To demonstrate their utility in E. coli-based protein overexpression.
- To highlight their application in probing protein-ligand interactions.
Main Methods:
- Development of novel heavy isotope-labeled amino acid precursors.
- Application in E. coli for metabolic protein labeling.
- Utilizing isotopologues for various Nuclear Magnetic Resonance (NMR) experiments.
Main Results:
- Achieved high selectivity and isotope incorporation levels in labeled proteins.
- Demonstrated low sample production costs, making NMR more accessible.
- Showcased the value of precursors in studying protein-ligand interactions.
Conclusions:
- The developed precursors offer an economical and efficient solution for protein labeling.
- These tools facilitate the routine use of protein NMR spectroscopy in drug discovery.
- Optimized protein samples enable detailed structural and dynamic analyses.
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