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Related Experiment Videos

Lanthanide-binding tags as versatile protein coexpression probes.

Katherine J Franz1, Mark Nitz, Barbara Imperiali

  • 1Department of Chemistry Massachusetts Institute of Technology Cambridge, MA 02139, USA.

Chembiochem : a European Journal of Chemical Biology
|April 3, 2003
PubMed
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New lanthanide-binding tags (LBTs) offer enhanced luminescence and affinity for Tb(3+) ions. This protein visualization tool accelerates gene sequence to protein function correlation in proteomic analyses.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Comprehensive proteomic analyses require advanced methods to link gene sequences with protein functions.
  • Biophysical probes that integrate into protein structures are crucial tools for these analyses.
  • Lanthanide-binding tags (LBTs) are fusion partners that bind lanthanide ions, offering luminescence, X-ray scattering, and magnetic properties.

Purpose of the Study:

  • To develop novel peptide sequences for lanthanide-binding tags (LBTs) with improved properties.
  • To demonstrate the utility of enhanced LBTs in protein visualization and analysis.

Main Methods:

  • Design and synthesis of new peptide sequences for LBTs.
  • Characterization of Tb(3+) ion binding affinity and luminescence intensity.

Related Experiment Videos

  • Fusion of LBTs to ubiquitin as a model protein.
  • Application of LBT-tagged proteins in SDS-PAGE and protein concentration determination.

    • Main Results:

    • Developed LBT peptides with 40-fold higher Tb(3+) affinity and significantly brighter luminescence.
    • Demonstrated rapid luminescence detection of LBT-tagged proteins in SDS-PAGE gels.
    • Enabled determination of protein concentrations in complex mixtures using LBTs.

    Conclusions:

    • The novel LBT strategy provides a powerful and accessible alternative for creating fluorescent fusion proteins.
    • Enhanced LBTs facilitate routine molecular biological techniques for protein visualization and analysis.
    • This approach accelerates the correlation of gene sequence with protein function in proteomic studies.