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Updated: Jun 16, 2026

Discovering Protein Interactions and Characterizing Protein Function Using HaloTag Technology
Published on: July 12, 2014
Lanthanide-tagged proteins--an illuminating partnership
Karen N Allen1, Barbara Imperiali
1Department of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, MA 02215-2521, USA. drkallen@bu.edu
Lanthanide-tagged proteins enable detailed studies of protein structure and function using X-ray crystallography and NMR. These lanthanide (Ln) probes offer new ways to understand complex biological processes at the molecular level.
Area of Science:
- Biochemistry
- Structural Biology
- Biophysics
Background:
- Lanthanide (Ln) ions possess unique properties valuable for studying proteins.
- Current methods for incorporating Ln ions include chemical modification or coexpression with binding tags.
Purpose of the Study:
- To highlight the utility of lanthanide-tagged proteins in structural and functional analyses.
- To discuss the application of Ln-tagged proteins in various biophysical techniques.
Main Methods:
- Chemical modification with synthetic lanthanide-chelating prosthetic groups.
- Coexpression of proteins with peptide-based binding tags for Ln complexation.
Main Results:
- Lanthanide tags provide heavy-atom sites for X-ray crystallography phase determination.
- Paramagnetic Ln ions in NMR yield distance constraints via residual dipolar couplings and pseudo-contact shifts.
- Lanthanide luminescence techniques aid in studying large protein complexes and dynamics in vivo.
Conclusions:
- Lanthanide-tagged proteins are versatile tools for protein structure, function, and dynamics investigations.
- These techniques enhance the understanding of cellular functions at the molecular level.
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