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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

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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...
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Tagging and Fusion Proteins01:24

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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...
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Labeling DNA Probes03:31

Labeling DNA Probes

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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...
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Related Experiment Video

Updated: Apr 15, 2026

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling
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Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

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Illuminating biological processes through site-specific protein labeling.

Gong Zhang1, Siqi Zheng, Haiping Liu

  • 1Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China.

Chemical Society Reviews
|April 11, 2015
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Summary

Site-specific protein labeling using genetically encoded tags or unnatural amino acids offers precise control. These advanced methods provide advantages over traditional fluorescent proteins for complex biological studies.

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Related Experiment Videos

Last Updated: Apr 15, 2026

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chemical Biology

Background:

  • Site-specific protein labeling is crucial for understanding biological processes.
  • Conventional methods like fluorescent proteins (FPs) have limitations in precision and versatility.
  • Genetically encoded peptide tags and unnatural amino acids (UAAs) offer alternative labeling strategies.

Purpose of the Study:

  • To review strategies for site-specific protein labeling using peptide tags or UAAs.
  • To highlight the advantages and necessity of site-specific labeling in biological research.
  • To introduce emerging dual site-specific labeling techniques.

Main Methods:

  • Utilizing genetically encoded peptide tags as labeling handles.
  • Employing unnatural amino acids (UAAs) for bioorthogonal labeling.
  • Discussing bioorthogonal reactions for precise protein modification.
  • Exploring single and dual site-specific labeling strategies.

Main Results:

  • Site-specific labeling provides precise control over protein modification sites.
  • These methods allow for a wide selection of labeling dyes.
  • Advantages over conventional fluorescent protein labeling are demonstrated.
  • Applications in solving complex biological problems are showcased.

Conclusions:

  • Site-specific protein labeling techniques are essential for advancing biological research.
  • Dual site-specific labeling strategies show significant potential for illustrating biological processes.
  • These methods offer superior control and versatility compared to traditional approaches.