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Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Labeling DNA Probes03:31

Labeling DNA Probes

DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Related Experiment Video

Updated: May 13, 2026

Preparation, Purification, and Characterization of Lanthanide Complexes for Use as Contrast Agents for Magnetic Resonance Imaging
13:21

Preparation, Purification, and Characterization of Lanthanide Complexes for Use as Contrast Agents for Magnetic Resonance Imaging

Published on: July 21, 2011

Noncovalent tagging proteins with paramagnetic lanthanide complexes for protein study.

Zhen Wei1, Yin Yang, Qing-Feng Li

  • 1State Key Laboratory of Elemento-Organic Chemistry and College of Chemistry, Nankai University, Tianjin, PR China.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|March 2, 2013
PubMed
Summary

Researchers developed a new method for protein labeling using paramagnetic lanthanide complexes. This technique enables precise structural analysis through noncovalent interactions, offering tunable properties for advanced NMR spectroscopy in structural biology.

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Preparation, Purification, and Characterization of Lanthanide Complexes for Use as Contrast Agents for Magnetic Resonance Imaging
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysical Chemistry

Background:

  • Site-specific protein labeling is crucial for NMR spectroscopy.
  • Paramagnetic lanthanides offer unique insights into protein structure.
  • Existing methods for lanthanide labeling can be complex.

Purpose of the Study:

  • To develop a novel, noncovalent method for site-specific protein labeling with paramagnetic lanthanides.
  • To explore the use of lanthanide-dipicolinic acid (DPA) complexes for generating paramagnetic restraints.
  • To demonstrate the tunability of binding affinity and paramagnetic properties.

Main Methods:

  • Synthesis of lanthanide-DPA complexes with varying ligand substituents.
  • Investigation of noncovalent interactions between these complexes and proteins.
  • Characterization of thermodynamic and paramagnetic properties.

Main Results:

  • Successfully formed noncovalent complexes between lanthanide-DPA derivatives and proteins.
  • Demonstrated that ligand substituents allow tuning of binding affinity and paramagnetic tensor.
  • Observed diverse thermodynamic and paramagnetic properties based on DPA derivative modifications.

Conclusions:

  • Noncovalent interactions provide an effective strategy for protein tagging with paramagnetic lanthanides.
  • This method facilitates the acquisition of multiple distance and angular restraints for protein structural analysis.
  • The tunable nature of the complexes enhances their utility in NMR-based structural biology.